Molecular Fluorescence, Phosphorescence, and Chemiluminescence

Anal. Chem. 2000, 72, 197R-209R

Molecular Fluorescence, Phosphorescence, and Chemiluminescence Spectrometry Philip B. Oldham,† Matthew E. McCarroll,‡ Linda B. McGown,§ and Isiah M. Warner*,‡

Department of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803, and Department of Chemistry, Duke University, Box 90346, Durham, North Carolina 27708-0346 Review Contents Books, Reviews, and Chapters of General Interest General Instrumentation Laser-Based Techniques Sensors Sample Preparation, Quenching, and Related Phenomena Data Reduction Luminescence in Organized Media Low-Temperature Luminescence Total Luminescence and Synchronous Excitation Spectroscopies and Related Techniques Solid Surface Luminescence Luminescence in Chromatography, Electrophoresis, and Flow Systems Dynamic Measurements of Luminescence Fluorescence Polarization, Molecular Dynamics, and Related Phenomena Chemiluminescence Near-Infrared Fluorescence Luminescence Techniques in Biological and Clinical Analysis Reagents and Probes Other Techniques and Applications Literature Cited

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This review covers the approximately two-year period since our last review (A1), roughly from November 1997 through October 1999. A computer search of Chemical Abstracts provided most of the references for this review. Coverage is limited to articles that describe new developments in the theory and practice of molecular luminescence for chemical analysis in the ultravioletvisible and near-infrared region. Citations may be duplicated between sections due to articles with contents that span several topics. However, in an effort to reduce the length of this review, we have tried to limit this kind of duplication. In general, citations are limited to journal articles and usually do not include patents, proceedings, reports, and dissertations. This review is considerably shorter than previous reviews. This is because we have tried to focus on important advances of general interest and relevance to the field of analytical chemistry rather than extensions of previous advances. This reduction was done at the request of the journal editor in an attempt to significantly reduce the length of the biannual reviews. We have also expanded †

Mississippi State University. Louisiana State University. § Duke University. ‡

10.1021/a1000017p CCC: $19.00 Published on Web 05/09/2000

© 2000 American Chemical Society

our description of individual citations for better clarification of content. Although we are not able to provide extensive coverage of developments of relevance to broad areas such as chromatography and biological sciences, we have tried to include major review articles and chapters relevant to these topics. However, if you feel that we have omitted an important article published during the above referenced time period, please forward the reference to one of us and we will be certain to consider it for the next review. BOOKS, REVIEWS, AND CHAPTERS OF GENERAL INTEREST Of significant interest is the publication of the second edition of Principles of Fluorescence Spectroscopy by Lakowicz (B1). This text quite nicely covers the many experimental and instrumental advances that have been made during the 16 years since the publication of the first edition. Also of general interest, and edited by the same author, is the publication of Topics in Fluorescence Spectroscopy: Nonlinear and Two-Photon-Induced Fluorescence, volume 5 of this series (B2). There were also several book chapters of interest published during this time period. Kettling and co-workers described a method using dual-color fluorescence cross-correlation spectroscopy for monitoring enzyme kinetics and activities (B3) and described its use in a rapid assay processing system (B4). Lakowicz and Gryczynski published a chapter reviewing multiphoton excitation of biochemical fluorophores (B5). There were several notable reviews published, most of which discuss biological applications of fluorescence spectroscopy. Weiss published a review of current advances in the detection of single biomolecules (B6). Wagnieres et al. published a comprehensive review of in vivo fluorescence imaging for oncological applications (B7), and Middendorf et al. reviewed near-infrared fluorescence instrumentation for DNA analysis (B8). Several reviews addressed fluorescence analysis in high-throughput screening (HTS). Silverman et al. published a general review of new assay technologies for high-throughput screening (B9), and Auer et al. published a more specialized review of miniaturized HTS apparatuses that employ fluorescence correlation spectroscopy (B10). In addition, a general review of HTS by Sittampalam et al. outlined advances in assay technologies (B11). There were two historical reviews reported. Nickel provided a chronological report of luminescence research prior to 1944, including a translation of Jablonski’s 1935 article, “On the mechanism of the photoluminescence of dye phosphors” (B12). Analytical Chemistry, Vol. 72, No. 12, June 15, 2000 197R

Schenk also published an historical review of fluorescence analysis through 1980 (B13). Other reviews reporting on the use of fluorescence included the use of fluorescent probes to study structural and functional aspects of enzymes (B14), proteins in sol-gel matrixes (B15), cellulose and lignin in mechanical pulps (B16) and the analyses of inorganic materials (B17). Kubista et al. published a review of chemometric methods to analyze spectroscopic data (B18). Sun et al. reviewed recent advances in the study of room-temperature protein phosphorescence (B19) and Potyrailo et al. published a review of the use of optical waveguide sensors in analytical chemistry (B20). GENERAL INSTRUMENTATION Several articles have addressed the continued need for calibration and spectral correction with standard spectrofluorometers. Zwinkels and Gauthier of the National Research Council of Canada have described a two-monochromator reference spectrofluorometer and associated calibration standards used for high-accuracy fluorescence measurements over the 250-1050-nm spectral range (C1). Instrument performance was demonstrated with various applications including paper, paint, and textile samples. Gardecki and Maroncelli have reported the use of six secondary emission standards that cover the 300-800-nm region for calibration of spectral responsivity (C2). A method for generating the spectral correction file with an accuracy of better than 10% over the entire wavelength range was described. Another report recently described the convenient use of three perylene derivatives as quantum yield standards (C3). All three exhibit photostability, quantum yields of 100%, only minor oxygen quenching, and good solubility in typical solvents. Kotelevskiy has reported a procedure for determination of the true refractive index for correction of fluorescence intensities with a commercial instrument (C4). Similarly, Credi and Prodi have described an easy-to-use method that accounts for instrumental factors and corrects the observed fluorescence intensities (C5). There have also been some significant improvements in instruments and instrumental components. Itami and Araki have developed a high-intensity, nanosecond, white light source, using a commercially available 150-W Xe arc lamp (C6). Pulses of 140 W (peak) and 15.2 ns (duration) were produced over a wavelength range of 250-650 nm. Also, a new rapid-scan monochromator has been reported for operation in the near-infrared spectral region (C7). Holst and co-workers have described the construction of a new modular luminescence lifetime imaging (MOLLI) system composed of a CCD camera with fast electronic shutter and a gated LED or arc lamp source (C8). The MOLLI system provides imaging of fluorescence lifetimes in the range of 1 ns to 1 s. A CCD camera is also an integral component in the recently developed instrument designed for microchip, parallel, hyperspectral fluorescence imaging associated with DNA microarray analysis (C9). Ratner and Haas have developed a new instrument incorporating temporal resolution both on the millisecond scale for changes in structural conformations and on the nanosecond scale for the dynamics of kinetic intermediates (C10). This has been accomplished by use of a single excitation pulse synchronized with a fast mixing stopped-flow device. Up to 20 fluorescence 198R

Analytical Chemistry, Vol. 72, No. 12, June 15, 2000

decay curves can be generated per second with temporal resolution of 0.5 ns. A new total internal reflection fluorescence (TIRF) spectrometer has been reported for the study of dynamic adsorption at liquid-liquid interfaces (C11). The spectrometer is designed to monitor fluorescence intensity changes over tenths of seconds while maintaining a stable optical focus on the fluid/ fluid interface for days at a time. The ability to conveniently acquire TIRF measurements at several different observation angles for depth profiling with quasi-temporal resolution has been reported by Shimosaka and co-workers (C12). A new mobile Lidar fluorescence instrument for environmental applications has been developed (C13). A two-channel instrument is described capable of shipboard monitoring of phytoplankton, turbidity, biomass productivity, and organic pollutants. Various instrument and method comparisons have been described including a procedure for comparing the features of commercial fluorescence spectrometers (C14). Oldham’s group has published a comparison of inner-filter effects for different cell configurations including conventional right angle, short-pass, front face, and TIRF (C15). Results showed significant improvements for concentrated and/or turbid samples by TIRF. The use of single-beam versus double-beam instruments for automatic correction in fluorescence excitation spectroscopy has been compared by Naqvi (C16). Enderlein and Kollner have compared the application of time-correlated single-photon counting with that of fluorescence correlation spectroscopy for single-molecule detection (C17). LASER-BASED TECHNIQUES Recently, considerable effort has been focused on the development of fluorescence correlation spectroscopy (FCS) and related techniques for studying the diffusion and association of macromolecules within a small volume. The technique is inherently laser-based and has particularly benefited from the development of two-photon excitation methods in microscopy. Visser and Hink have outlined the basic principles of FCS and reported a comparative study with time-resolved fluorescence anisotropy (D1). Other potential applications of FCS were also presented. Harris’s group at the University of Utah has reported the use of patterned photoexcitation with FCS (D2). This is accomplished using two, intersecting, coherent laser beams to create an interference fringe pattern from which fluorescence fluctuations can be observed. Hattori and Shimizu have performed a similar experiment using a traveling interference fringe pattern created using an acoustooptic modulator (D3). Gratton’s group at the University of Illinois has described the photon-counting histogram (PCH) method for extracting photon counts per molecule and average number of molecules within the observation volume from FCS experiments (D4). Two separate groups have recently reported multiphoton excitation and fluorescence emission of nonaromatic hydrocarbons. Lakowicz’s group has demonstrated two-photon excitation and subsequent time-resolved emission of dioxane using picosecond pulses at 380 nm (D5). Similarly, Volkmer and co-workers recently described the multiphoton excitation of several linear and cyclic saturated hydrocarbons in neat solution using a femtosecond laser at 800 nm (D6). The ability to monitor individual labeled lipid molecules within a membrane has also been reported using

two-photon excitation and wide-field epi-illumination (D7). The authors suggest the ability to image single molecules on native cell membranes may soon be possible. More traditional applications of lasers for fluorescence spectroscopy continue to appear in the literature as well. Lohmannsroben and co-workers have reported the use of laser-induced fluorescence (LIF) for in situ analysis of petroleum products in soils (D8). Similarly, Rudnick and Chen have described the application of LIF for detection and quantification of polycyclic aromatic hydrocarbons in seawater and sediments (D9). Ha and co-workers have reported the use of single-molecule fluorescence polarization anisotropy and single-pair fluorescence resonance energy transfer for determining molecular distances and orientations with proteins and nucleic acids (D10). A novel application of fluorescence line-narrowing (FLN) spectroscopy has been presented by Larsen and co-workers (D11). They were able to directly identify pyrene metabolites within the gut organs of terrestrial isopods by collecting FLN spectra from the frozen organs at 11 K. SENSORS Work in the development of luminescence-based sensors for industrial, biological, or environmental applications continues to appear frequently in the literature. Manyam and co-workers have developed a bifurcated fiber-optic pH sensor incorporating a porous sol-gel coating (E1). The sol-gel is doped with a fluorescein derivative that exhibits spectral sensitivity over a wide pH range. A fiber-optic sensor for dissolved oxygen in commercial fish ponds has been described by Asundi and co-workers (E2). Here a ruthenium complex sensitive to O2 fluorescence quenching is attached to the end of the fiber probe. A comparison to a conventional electrochemical O2 sensor for miniaturization and field use was discussed. Lo and co-workers have reported a new, water-soluble phosphor for in vivo oxygen measurements in animals (E3). An excellent fit to Stern-Volmer quenching with large lifetime changes is observed over a wide range of physiologically relevant temperatures. A large Stern-Volmer constant was also observed for C70, providing the basis for a novel oxygen sensor device (E4). Krause et al. reported development of a luminescence decay time-based K+ ion sensor to overcome pH cross-reactivity and optical interferences associated with intensitybased K+ sensors (E5). Blue and co-workers have described a minimally invasive optoelectronic technique for the chemical analysis of aqueous humor (E6). A fiber-optic method for LIF identification and quantification of marine pollution has been reported (E7). Timeresolved spectroscopy was used to resolve a mixture of anthracene and pyrene as a model for gasoline and jet oil in water. A fiberoptic device for the in situ determination of organic pollutants in soil has been described by Moser-Boroumand and co-workers (E8). Two different probe designs were evaluated along with probe location. Luminescence sensors based on planar waveguides or disposable “chips” are continuing to gain in popularity. Meusel and coworkers have developed a disposable, low-cost sensor chip for environmental analysis of the popular herbicide 2, 4-D (E9). The method incorporates microfluidic sample handling with optical readout using NIR-TIRF. The evanescent wave excitation elimi-

nates the necessity of any washing or separation steps. Asanov and co-workers recently demonstrated a regenearable biosensor platform based on TIRF detection coupled to electrochemical control of the sensor surface (E10). Electrochemical polarization was shown to effectively modulate otherwise kinetically irreversible biospecific interactions such as biotin-streptavidin and biotin-antibiotin. SAMPLE PREPARATION, QUENCHING, AND RELATED PHENOMENA Several papers have focused on advances in fluorescence analysis using quenching techniques. Goodpaster and McGuffin have developed a novel system for rapid determination of SternVolmer quenching constants (F1). The system relies on automated sample mixing using capillary flow injection. The small size of the capillary eliminates the need to for inner-filter corrections. Ayala et al. reported the development of a method for the determination of fluorene in cetylpyridinium bromide micelles using a synchronous scanning method (F2), and Gao et al. reported a catalytic quenching method for the determination of vanadium (F3). The quenching of triplet states by molecular oxygen was investigated by Wilkinson and Abdel-Shafi (F4), and Cioni and Strambini reported the use of room-temperature tryptophan phosphorescence to monitor structural fluctuations in proteins (F5). Acrylamide quenching was used to evaluate structural fluctuations of the globular fold. Advances in sample analysis include a study by Nygren et al. in which they demonstrate a method whereby unambiguous characterization of a single sample is achieved using fluorescence spectroscopy and solvent extraction (F6). Advances in oxygen sensing have been reported by Potyrailo and Hieftje (F7). They have developed a fiber-optic sensor based on the quenching of tetraphenylporphyrin that has been immobilized in the cladding of the fiber. DATA REDUCTION There were several papers published concerning the use of artificial neural networks and chemometrics. Suarez Araujo presented a theoretical study of the application of artificial neural networks in luminescence spectroscopy (G1). Another study by Todeschini and Galvangi reported the use of artificial neural networks to select optimal wavelength sets for partial least-squares analysis (G2). Also reported was a study by Ferrer et al. that used artificial neural networks to analyze polycyclic aromatic hydrocarbons (PAHs) in water by synchronous fluorescence (G3). A general article by Munck et al. has appeared that demonstrated the feasibility of chemometrics in food science (G4), and Bro used multivariate statistics in an exploratory analysis of sugar production (G5). Prakash et al. reported an optical regression method for quantitative analysis in single-channel spectrometers (G6). The theory of optical regression is presented and its precision compared to that of digital regression procedures. Dufour and Riaublanc reported an interesting application of fluorescence using front-face illumination (G7). In this study, raw, heated, and homogenized milks were distinguishable by use of a combination of fluorescence spectroscopy and chemometric techniques. Villegas and Neal presented a paper describing the analysis of pyrene photokinetics in sodium dodecyl sulfate (SDS) micelles (G8). Matrix-formatted wavelength-dependent frequency domain fluorescence was subjected to frequency domain analysis that was Analytical Chemistry, Vol. 72, No. 12, June 15, 2000

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model independent. Pseudorank estimation was used to estimate the number of fluorescent components in pyrene/SDS solution. LUMINESCENCE IN ORGANIZED MEDIA Several studies have investigated luminescence phenomena in organized media. These include studies in micellar, macrocyclic, and sol-gel media. Garg et al. have reported the determination of zinc(II) using N-(2′-pyridyl)-2-hydroxybenzamide in a Brij-35 micellar medium (H1). Another study by Wang et al. reported the simultaneous detection of niobium, tantalum, and zirconium using morin in a micellar medium (H2). Partial least-squares analysis was used to circumvent problems of spectral overlap. Two studies reported luminescence studies of PAHs in micellar media. Pandey et al. reported a comprehensive study of the quenching effects of cetylpyridium ion on PAHs in mixed-surfactant systems (H3). Romanovskaya et al. developed a method optimizing roomtemperature phosphorescence for the detection of PAHs in micellar systems (H4). Similarly, Hagestuen Campiglia have described a new method for screening water samples for PAHs using a combination of solid-phase extraction and room-temperature phosphorimetry (H5). There were several studies that reported the use of fluorescence in the characterization of micellar systems. Rawat and Chattopadhyay monitored structural transitions in SDS micelles using fluorescent probes located in different parts of the micelle (H6). McCarroll and co-workers have investigated the phenomenon of preclouding in solutions of nonionic surfactants using steady-state and time-resolved anisotropies of intrinsic and probe fluorescence (H7-H9). Billiot et al. published a study using fluorescent probes to characterize the microenvironment of polymeric micelles composed of various chiral dipeptide surfactants (H10). Other investigations of micellar systems include studies of indigo carmine dye in micellar and cyclodextin media (H11) and a study of enzyme solubilization in Aerosol-OT reverse micelles (H12). Additional studies used fluorescence spectroscopy to characterize complex formation in micellar systems. Polewski Napierala reported a study of amylose-dye complexes in cationic micelles (H13). Fluorescence spectroscopy was used to determine the association constants and the critical micelle concentrations of the surfactants in the presence of the dye. Munoz et al. reported on the effects of cationic micelles on the formation of ternary oxalate complexes (H14). Of particular interest is a study by Villegas and Neal that examined pyrene eximer kinetics in micellar solutions of SDS (H15). The popular use of pyene as a probe makes this study particularly important. The authors acquired dynamic multidimensional fluorescence data matrices, which were then subjected to rank analysis. The results of this study indicate that pyrene exists in three distinct forms, supporting a proposed three-state model. Several investigations involving cyclodextrins were also reported. A report by Pistolis discussed dual excimer emission by p-terphenyl in the presence of γ-cyclodextrin (H16). Escandar published a report of the spectrofluorometric determination of piroxicam in the presence of β-cyclodextrin, including a determination of the complex stoichiometry and its association constant (H17). Liu et al. have developed a method utilizing a β-cyclodextrin-hemin complex for the determination of hydrogen peroxide 200R


(H18). Datta et al. have investigated the interaction of the surfactant Triton X-100 with cyclodextrins and report a greater degree of interaction with β-cyclodextrin than with R-cyclodextrin (H19). Additional studies involving cyclodextrins include an investigation of cyclodextrin-complexed cadmiun sulfide particles (H20), the encapsulation of podands by β- and γ-cyclodextrins (H21), and the complexation of 2-(4′-aminophenyl)- and 2-(4′-(N,Ndimethylamino)phenyl)benzothiazole with β-cyclodextrin (H22). Other studies in organized media include an investigation of the spectral properties of Sn(IV) tretrapyridyl and tetramethylpyridium porphyrins in sol-gel matrixes (H23). Another solgel study by Hartnett et al. investigated the kinetics and thermodynamics of flavins within glucose oxidase (H24). Also of interest is a study by Yan and Myrick in which they demonstrate the simultaneous enantiomeric determination of dansyl-D,L-phenylalanine in the presence of R-acid glycoprotein (H25). Zhang et al. have investigated formation of complexes of the dye brilliant cresyl blue and a sulfonated calix[4]arene (H26) and auramine O with a sulfated calix[6]arene (H27). Another study by Grady et al. used fluorescence quenching to demonstrate chiral resolution using (S)-dinaphthylprolinol calix[4]arene, as well as its ability to perform enantiomeric separations in CE when immobilized to the capillary wall (H28). There were several studies that examined humic materials. Engebretson and von Wandruszka have reported on the kinetics of aggregation in humic acids, showing evidence for slow and reversible formation of pseudomicellar pockets (H29). Similarly, Sharpless and McGown have examined the effects of aluminuminduced aggregation on the fluorescence properties of humic substances (H30). A presentation of evidence supporting the micellar model of humic acid was published by von Wandruszka (H31). LOW-TEMPERATURE LUMINESCENCE Not much activity was evident in low-temperature luminescence analysis. Benzo[a]pyrene was determined in drinking and natural waters using low-temperature luminescence with and without preliminary chromatographic fractionation on an unfixed bed of aluminum oxide (I1), which yielded results containing significant deterministic irreducible and random systematic errors. Steps were taken to determine the sources of error and conditions for optimization were suggested. Shpol’skii excitation spectra of single-impurity molecules of terrylene in n-decane at 1.7 K were collected with high spectral resolution and good quality (signalto-noise ratio up to 15) (I2), and single-molecule spectroscopy of terrylene in n-alkane mixtures was studied to determine whether special Shpol’skii guest-host combinations that exhibit welldefined trapping sites are essential for single-molecule spectroscopy (I3). TOTAL LUMINESCENCE AND SYNCHRONOUS EXCITATION SPECTROSCOPIES AND RELATED TECHNIQUES The development of total luminescence and synchronous excitation techniques continues to be well represented in the literature. Li and co-workers described a theoretical basis for calculation of peak location, intensity, and bandwidth associated with synchronous fluorescence spectra (J1). The approach provides a theoretical guide for the design of both constant-

wavelength and variable-angle synchronous fluorescence experiments. A portable synchronous scanning luminoscope (SSL) has been reported for on-site analysis of contaminated soil and groundwater (J2). The SSL is capable of quantitative analysis of complex mixtures of creosotes, PCBs, and PAHs. Both total luminescence and synchronous excitation have been reported for environmental studies with natural organic matter (NOM). Synchronous fluorescence has been reported for the examination of carbamate pesticide binding to dissolved organic matter (J3). Conditional binding constants, determined by fluorescence quenching, were used to predict potential drainage transport. Total luminescence has been used to examine spectral differences among various samples from the Scandanavian NOM typing set and their aluminum complexes (J4). Smith and Kramer have reported a revised method for determination of conditional binding constants and site concentrations for aluminum and NOM using total luminescence spectroscopy and multiresponse parameter estimation (J5). Several reports have appeared on the use of synchronous fluorescence for clinical or pharmaceutical formulation analysis. Second-derivative synchronous fluorescence spectra were used by Ruiz and co-workers for the analysis of binary mixtures of nonsteroidal antiinflammatory drugs based on their intrinsic fluorescence in chloroform (J6). Murillo Pulgarin and co-workers have reported the use of first-derivative, nonlinear variable-angle synchronous fluorescence for the simultaneous determination of atenolol, propranolol, dipyridamole, and amiloride in a fourcomponent mixture (J7). Nonlinear variable-angle synchronous fluorescence has also been combined with partial least-squares regression type 1 for the simultaneous determination of a threecomponent mixture of pyridoxal, pyridoxamine, and pyridoxic acid at low-ppb concentrations (J8). Sabry has described the application of a computerized compensation method to derivative synchronous fluorescence for simultaneous determination of floctafenine and its major metabolite in plasma samples (J9). Total luminescence and synchronous scanning have also been applied to environmental analyses. Ferrer and co-workers have applied partial least-squares analysis to resolve the synchronous fluorescence spectra of a 10-component mixture of PAHs (J10). Selective quenching has also been combined with synchronous fluorescence to reduce the spectral complexity of multicomponent samples (J11). Rank annihilation factor analysis has been reported with total luminescence spectroscopy for the analysis of complex environmental samples (J12). In this case, a simulated 15component mixture demonstrates the method capabilities. However, as reported, interferences from the ubiquitous humic substances and increased scattered light in natural water or soil samples limit the technique. A relatively new application for total luminescence and synchronous fluorescence is in the burgeoning area of biotechnology. Marose and co-workers have described the use of two-dimensional fluorescence spectroscopy as a new method for real-time bioprocess monitoring of cell growth (J13). Cell growth and cellular metabolism, shift from aerobic to anaerobic conditions, and uncoupling of the oxidative phosphorylation could be detected. This same group also reported development of a two-dimensional fluorescence sensor for on-line bioprocess monitoring (J14, J15). The group at Sandia National Laboratory has investigated the

extent of distinguishability and biological variability for the fluorescence spectra of complex biological specimens (J16). Chen and co-workers have described the use of intrinsic total luminescence spectra from tryptophan residues for the study of conformational changes in the protein hemorrhagin III (J17). These data confirmed that the tryptophan residues were mainly located in hydrophilic regions at the protein surface. Yang and co-workers have reported the first synchronous fluorescence spectra for hemoglobin solutions (J18). The affect of concentration on the spectra was studied along with the influence of molecular aggregation. SOLID SURFACE LUMINESCENCE A number of agricultural and clinical applications of solid surface luminescence have recently appeared in the literature. Front-surface fluorescence of cereal flours with the potential for distinguishing different species of cereals and even cultivars has been reported (K1). Variable-angle, front-face fluorescence has also been reported for the characterization of milk (K2). Principal component analysis was utilized to discriminate between heated and homogenized milk samples. Billa and co-workers have demonstrated the ability of solid surface fluorescence of paper pulps with principal component analysis to provide information about the origin of the pulp, type of pulping method used, and lignin content (K3). A method for the determination of the pesticide thiabendazole in various raw vegetables and different types of water by solid surface room-temperature phosphorescence (RTP) has been reported (K4). The simple method was shown to be selective and sensitive down to ppb levels. The same group also published the simultaneous determination of two pesticides, thiabendazole and carbaryl, by solid surface RTP, and partial least-squares analysis (K5). Campiglia and Vo-Dinh have demonstrated the use of RTP on filter paper for the analysis of cocaine and benzoylecgonine in saliva samples (K6). Kitade and co-workers have determined p-aminobenzoic acid (PABA) in the presence of serum albumin by RTP on a poly(vinyl alcohol) substrate (K7). The albumin was unable to penetrate into the substrate and allowed RTP from the PABA to be selectively detected from the backside of the substrate. The simultaneous determination of three anthracyclines has been reported using time-resolved, solid surface RTP (K8). Kalman filtering was used to analyze the time-resolved RTP data. Hurtubise’s group has produced several recent reports on the solid-matrix fluorescence and phosphorescence of benzo[a]pyrene-DNA adducts. Initially, various methods of solid-matrix luminescence were investigated to help selectively distinguish various adduct forms (K9). Quantitative comparisons between solid-matix fluorescence and phosphorescence have been reported (K10). Limits of detection down to picogram levels were observed with solid-matrix phosphorescence. Most notably, a linear relationship has been observed between solid-matrix phosphorescence and the percentage of DNA modification (K11). In this case, 2 adducts out of 107 bases has been determined to be the limit of detection. Hurtubise’s group has also reported on the use of hydrophobic filter paper for combined solid-phase microextration and subsequent solid-matrix luminescence measurements (K12, K13). This has been demonstrated by extracting a set of 10 PAHs from water Analytical Chemistry, Vol. 72, No. 12, June 15, 2000

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and determining their respective distribution constants. Mixtures of up to four components were resolved by combination of solidmatrix fluorescence and phosphorescence spectra with detection limits at the low parts-per-trillion level. Ramasamy and Hurtubise have described a relatively simple oxygen sensor based on oxygen quenching of RTP from perdeuterated phenanthrene adsorbed on Whatman 1PS filter paper (K14). LUMINESCENCE IN CHROMATOGRAPHY, ELECTROPHORESIS, AND FLOW SYSTEMS Several studies have involved fluorescence detection in liquid chromatography. Weinmann et al. reported the simultaneous determination of retinol and tocopherol using fluorometry and ultraviolet absorption, respectively (L1). Lechowicz and Wojciech reported a method for the determination of LSD in biological fluids using HPLC with fluorescence detection (L2). Beltran et al. have developed a multivariate calibration procedure that relies on fastscanning fluorescence detection (L3). In this method, a threedimensional data set is collected that represents the emission wavelength, emission intensity, and retention time. Moutiez et al. reported the use of time-resolved luminescence as a detection mode for gadolinium (L4). Other uses of fluorescence in HPLC separations include the determination of nitrite in water via reaction with N-methyl-4-hydrazino-7-nitrobenzofuranzan (L5). Benito et al. have developed a capillary electrophoresis (CE) technique for the determination of bovine whey proteins using on-column derivatization and LIF detection (L6). Van Orden et al. have used the technique of fluorescence correlation spectroscopy as a detection scheme in CE (L7). Fuller et al. reported a method of single-neuron analysis that uses nanoliter volume sampling, CE separation, and wavelength-resolved fluorescence detection (L8). Additional improvements in fluorescence detection have been reported by Fultz et al. where they demonstrate timeand wavelength-resolved fluorescence detection in capillary zone electrophoresis using axial laser excitation within the capillary (L9). Shamsi et al. have used indirect laser-induced fluorescence detection for the analysis of anions in capillary electrophoresis (L10). He et al. demonstrated the use of on-the-fly fluorescence lifetime detection of labeled DNA primers in capillary gel electrophoresis (L11), and Li and McGown have investigated the effects of gel material on fluorescence lifetime detection in these systems (L12). Several studies have used fluorescence detection in combination with flow analysis. The determination of aluminum in beverages using lumogallion as a complexing agent (L13) and the speciation of thallium by flow injection analysis (FIA) with fluorescence detection (L14) have been reported. In addition, a method for the FIA of paraquat using fluorescence detection has been described (L15). Smith et al. have described the use of fluorescence detection in super critical fluid separations using a packed bed column (L16). DYNAMIC MEASUREMENTS OF LUMINESCENCE In a theoretical work (M1), an explicit expression was derived for the probability distribution of the amplitudes of the biexponential fluorescence decay of a two-state system observed in singlemolecule experiments of finite duration. It was found that, when the interconversion rates in the ground and excited states differ, the single-molecule and bulk experiments will give different results 202R


even in the limit of infinite duration of the experiment. In a study of phosphorescence decay (M2), a model was presented to explore the effects of flash duration on the shape of the emission curve obtained from systems exhibiting continuous heterogeneity of quencher concentration. Additionally, a procedure was described to convert the distribution of reciprocal lifetimes into a volume distribution of quencher concentration. Results showed that differences in initial intensities between compartments with different quencher concentrations must be considered in interpretation of quenching results and that the differences in initial intensity decrease with decreasing flash duration. As is often the case, much of the activity in dynamic measurements has involved biological systems. A study of a complex formed between β-lactoglobulin and 1-anilinonaphthalene-8-sulfonate (ANS) using steady-state and dynamic fluorescence titrations showed that the binding strength is strongly influenced by pH and ionic strength (M3). Bound ANS exhibited biexponential decay that suggests two different binding sites or binding modes. The results of this study indicate that electrostatic interactions are important in ANS binding to the protein. In another study, frequency domain fluorescence spectroscopy was used to study changes in conformation and environment associated with the interaction of single-tryptophan amphipathic peptides with a phospholipid surface (M4). Time-resolved fluorescence polarization was used to study FAD of tetrameric NADH peroxidase from Enterococcus faecalis and three mutant enzymes (M5). The amino acids that were responsible for the strong dynamic quenching of flavin fluorescence were identified. The observation of rapid, nanosecond depolarization due to excited-state charge transfer between Tyr-159 and flavin was related to a change of transition moment out of the plane of the isoalloxazine ring and identified as an unusual source of fluorescence depolarization. In the area of chemical analysis, time-resolved spectroscopy of minerals including natural apatite, scheelite, zircon, calcite, and fluorite was used to detect the luminescence centers which could not be resolved using steady-state measurements (M6). Luminescence of rare-earth elements that had been obscured by stronger bands of other emitters could be resolved, allowing detection of Pr3+, Tm3+, and Er3+ in minerals and also in the presence of Sm3+, Dy3+, and Tb3+, which are interfering ions with similar emission spectra. Time-resolved spectroscopy was used to study a hematoporphyrin derivative (HPD), Photosan-3, which is used as a photosensitizer in photodynamic therapy of tumors (M7). The results confirmed results for other HPD which indicated that aggregates and dimers are probably more responsible for the photodynamic effect than monomers. FLUORESCENCE POLARIZATION, MOLECULAR DYNAMICS, AND RELATED PHENOMENA The use of polarization spectroscopy to probe the rotational dynamics of single fluorescent molecules was reviewed (N1) and included discussions of molecules immobilized on dry surfaces, an aqueous environment, DNA-tethered fluorophores in aqueous environments, and protein-conjugated fluorophores. In a related paper, fluorescence polarization anisotropy was used along with fluorescence resonance energy transfer to investigate single molecules of staphylococcal nuclease (I) (N2). The results

revealed patterns of fluctuations that may arise from protein conformational dynamics on the millisecond time scale and information about the dynamic interactions of the enzyme with single substrate molecules. The dynamic properties of the R-subunit of tryptophan synthase from Escherichia coli were studied using time-resolved fluorescence anisotropy (N3). The rotational correlation time of 1-anilino8-naphthalenesulfonate that was bound to nonpolar surfaces of folding intermediates provided insight into the refolding reaction of the protein subunit. In another study (N4), fluorescence polarization, along with energy transfer and quenching, was used to provide evidence of direct physical association between intact 70S E. coli ribosome particles and denatured horseradish peroxidase during refolding of the protein. On the basis of the polarization measurements, the Kd of the complex was estimated to be 41 nM. Polarized phosphorescence from a triplet probe, erythrosin-5-iodoacetamide, was used to study the microsecond rotational dynamics of complexes of rabbit skeletal and cardiac muscle tropomyosin with F-actin (N5). The extrinsic probe was attached to sulfhydryls in the tropomycins. The roughness of water/carbon tetrachloride and water/1,2dichloroethane interfaces was studied using time-resolved total internal reflection fluorometric measurements of the dynamic fluorescence anisotropy of Sulforhodamine 101 and excitation energy transfer from Sulforhodamine 101 to Acid Blue 1 (N6). Results indicated that rotational reorientation of Sulforhodamine 101 at the water/CCl4 interface was restricted in the twodimensional plane of the interface, while that at the water/1,2dichloroethane interface resembled reorientation in an isotropic medium. The water/1,2-dichloroethane interface appeared to be rough compared to the water/CCl4 interface. Fluorescence correlation spectroscopy and time-resolved fluorescence anisotropy were used to investigate the dynamic properties of two BODIPYlabeled phospholipids in various micellar systems (N7). The probe was shown to significantly affect the self-assembly behavior of the detergents in the micellar media, which was attributed primarily to lateral diffusion of the probe in certain detergents (Triton X-100, Thesit, CTAB, SDS) but not in the more rigidly packed micelles apparently formed by digitonin and deoxycholate molecules. CHEMILUMINESCENCE Cherednikova et al. have described a comparative study of different types of luciferases (O1), and Arakawa et al. have developed a chemiluminescent assay for β-D-galactosidase (O2). Additional developments in chemiluminescent analysis include the photographic detection of fluorescent-labeled oligodeoxynucleotide by peroxyoxalate luminescence (O3). Traykov et al. reported a study of the release of superoxide radical in rat peritoneal macrophages (O4). NEAR-INFRARED FLUORESCENCE Several new near-infrared (NIR) fluorescence probes have been reported. Kukrer and Akkaya have synthesized and characterized a novel squaraine derivative with two phenylboronic acid functional groups (P1). The molecular probe is useful for NIR fluorescence detection of carbohydrates in aqueous solutions. Gallaher and Johnson have synthesized a polymethine cyanine NIR label for derivatization of fatty acids in capillary electrophoresis (P2). Baars and Patonay have evaluated a new NIR fluorescent dye for

ultrasensitive detection of peptides with capillary electrophoresis (P3). The observed dynamic range was linear over more than 2 orders of magnitude, and the limit of detection was a few hundred zeptomoles. The potential for synthesis of NIR fluorescence imaging probes with specificity for particular enzymes in living organisms has been described by Tung and co-workers (P4). Hofstraat and co-workers have reported the sensitized NIR fluorescence of various rare earth ions using a fluorescein derivative with excitation in the visible wavelength range (P5). This approach can provide long excited-state lifetimes and large absorption cross sections. Tarazi and co-workers have characterized the spectral behavior of a novel NIR cyanine dye, TG 170, and studied its complexation with metal ions (P6). A novel investigation has been described on the use of NIR fluorescence to detect Alzheimer’s disease in living patients by brain tissue autofluorescence (P7). Since the NIR wavelengths can effectively penetrate through skull and overlaying tissue, there is potential for development of a noninvasive clinical diagnostic. Spectral data calibrated with principal component analysis indicate correlation with clinically significant information. Soper’s group at Louisiana State University has been particularly active in development of NIR fluorescence techniques for analysis of oligonucleotides. They have reported the use of a series of NIR fluorescent dyes for base-calling in a single-lane DNA-sequencing format (P8). The dyes contained different intramolecular heavy atoms for altering the excited-state lifetimes. Although the fluorescence lifetimes varied considerably, no appreciable difference in spectral behavior, quantum efficiencies, or electophoretic mobilities was observed. They have also described nanoliter-scale NIR fluorescence for oligonucleotide detection on plastic microchips and gel-filled capillaries (P9). Middendorf and co-workers have produced a review of NIR fluorescence instrumentation for DNA analysis (P10). Soper’s group has recently reported a simple NIR timecorrelated single-photon-counting instrument for microscopic scanning applications (P11). The device exhibited good stability in the spatial scanning mode, detection sensitivity of 0.5 nM, and lifetime detectability down to 500 ps. They have also constructed a fiber-optic-based multichannel NIR time-correlated single-photoncounting instrument using a passively mode-locked Ti:sapphire laser and three single-photon avalanche diode detectors (P12). Patonay’s group has developed a NIR fluorescence, fiber-optic immunosensor (P13). In addition, they have designed a simple and reliable interface between a high-sensitivity NIR fluorescence detector and a commercial capillary electrophoresis system (P14). LUMINESCENCE TECHNIQUES IN BIOLOGICAL AND CLINICAL ANALYSIS A review of fluorescence correlation spectroscopy to observe molecular interactions in their natural environment, on cell surfaces, or in cytoplasm was presented (Q1). The fluorescence correlation technique, which employs time-resolved measurements of fluorescence emission, was used to investigate the pH dependence of conformational fluctuations of green fluorescent protein mutants in small ensembles of molecules in solution (Q2). The time-resolved measurements monitored fluctuations in the protonation state of the chromophore and the autocorrelation function of fluorescence emission revelaed contributions from two chemical Analytical Chemistry, Vol. 72, No. 12, June 15, 2000

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relaxation processes as well as diffusional concentration fluctuations. The use of luminescence spectroscopy to study biological membranes continues. Wavelength-selective fluorescence was investigated as a tool for studying the depth of membrane penetration of a reporter fluorophore (Q3). Chemically identical fluorophores that differed only in their penetration depths in a membrane showed different wavelength-dependent fluorescence parameters (spectra, polarization, lifetime, rotational correlation times), which indicated differences between their chemical microenvironments. The differences were attributed to different rates of solvent relaxation at the different penetration depths. A variety of luminescence studies involved proteins. Affinity tags were used to reversibly attach receptor proteins to a quartz surface, to detect real-time binding of ligands to membrane receptor proteins for screening of ligands for membrane protein receptors by total internal reflection fluorescence (Q4). Binding affinities, kinetic parameters of binding, and potential interferences were investigated. β-Sheet protein structures above the critical protein aggregation concentration were studied using timeresolved fluorescence spectroscopy of a cyanine dye, along with absorbance and fluorescence spectral measurements (Q5). Increases in fluorescence quantum yield and lifetyime of the dye were observed in the presence of β-sheet protein in aqueous solution. A membrane-permeant fluorescein derivative was used to label recombinant proteins containing four cysteines in the R-helix in living cells (Q6). The dye, which was administered extracellularly, is nonfluorescent until it binds to the tetracysteine domain. Advantages over green fluorescent protein were discussed. Several studies involving DNA and RNA have recently been published. The geometry of molecular binding to carrier molecules was studied using stereoisomers of benzo[c]chrysene diol epoxide as the molecular tags and DNA as the carrier (Q7). The geometry of the optical moments of the DNA tags was determined using electrofluorescence polarization spectroscopy, which measures the polarized fluorescence from the bound tag molecules and the changes that occur with electric field alignment of the carriers. An effort to isolate RNA motifs that can bind to fluorescent labels yielded two aptamers that recognize sulforhodamine B and one aptamer that recognizes fluorescein (Q8). One of the sulforhodamine B-binding aptamers was found to contain an unusually large motif of approximately 60 nucleotides and recognize both the planar aromatic ring system and a negatively charged sulfonate. The aptamers to the two dyes were able to discriminate between the dyes, as evidenced by localization of each fluorophore to beads tagged with the corresponding aptamer. In another aptamer-related study (Q9), interactions between DNA oligomers and fluorescent DNA indicator dyes were studied. Conformational differences among four oligonucleotides of different sequence and structure, including two that form a G-quartet and two that do not, were noted, including significant differences among the dye interactions and binding stoichiometries. In another study (Q10), fluorescence energy transfer and fluorescence correlation spectroscopy were used to investigate the kinetics of DNA hairpin-loop fluctuations. Results indicated that the rate of unzipping of the hairpin stem is essentially independent 204R


of the characteristics of the loop, whereas the rate of closing varies greatly with the loop length and sequence. In the area of DNA hybridization detection, a method was described in which time-resolved fluorescence measurements were used in a sandwich-type hybridization assay for simultaneous detection of up to six oligonucleotides from a single sample (Q11). The hybridization probes were assembled on particles, and after hybridization, each individual particle was subjected to three different measurements: the intensity of the prompt fluorescence signals of fluorescein and dansyl defined the particle category, while emission from a europium(III) chelate quantified the hybridization. Two papers involved the dye berberine, which increases its fluorescence quantum efficiency by a factor of 25-30 upon binding to nucleic acids. One of the papers investigated the spectroscopic and binding properties of berberine (Q12) and found evidence for groove binding rather than intercalation. A limit of detection of 12 ng/mL was reported for calf thymus DNA using berberine as the indicator. The other paper also reported on DNA detection using berberine (Q13), noting that the dye can be used to detect DNA or RNA over a wide pH range and without disrupting the native structure of DNA and RNA. Several fluorescence-based techniques were reported for biological analysis. A technique was described for high-throughput screening using confocal fluorescence to measure fluorescence fluctuations that occur coincidently in two different spectral ranges from a subfemtoliter observation volume (Q14), to monitor whether an association between molecular fragments that are labeled with different fluorophores is established or broken. A phase-modulation, fluorescence lifetime-based homogeneous fluoroimmunoassay for 2,4-dichlorophenoxyacetic acid was reported (Q15). Fluorescence spectroscopy was used to detect PrPSc, which is a protease-resistant form of a host-coded glycoprotein, to detect PrPSc, and to distinguish between different forms of the prion protein (Q16). Identification and discrimination of PrPSc is related to diagnosis of prion diseases and was based on spectral signatures and calculations of fluorescence cross sections. The absorption and luminescence spectral characteristics of amniotic fluids were investigated (Q17) and were found to exhibit changes related to the health of the pregnancy. Spectral shifts to longer wavelengths were observed in the luminescence spectra of the amniotic fluid in cases of intrauterine fetation pathologies compared to normal pregnancy cases. The detection of bacterial endospores using a terbium cation was reported (Q18, Q19). The terbium cation forms a luminescent complex, terbium dipicolinate, upon reaction with dipicolinate anions released from bacterial spore cases. Sources of interferences to generate false positive or negative results were evaluated. REAGENTS AND PROBES Several studies involved the use of fluorescence measurements of oligonucleotide binding. In one case, two complementary oligodeoxyribonucleotide hexamers and a pentamer with a fluorescent nucleoside incorporated into it were synthesized and characterized by spectroscopic and chromatographic studies (R1). The effect of incorporation of the fluorescent nucleotide into the sequence and its subsequent hybridization with the complementary sequence were studied.

In another study (R2), it was shown from the UV melting behaviors that pyrene-modified oligonucleotides could bind to both their complementary DNA and RNA in aqueous solution. The pyrene-modified oligonucleotides showed higher affinity for DNA but lower affinity for RNA, compared to the unmodified oligonucleotides. The pyrene-modified oligonucleotides exhibited pyrene monomer emission, and the fluorescence intensity ratio of band III/band I was increased upon binding to DNA. In addition, exciplex emission was also observed. Binding to RNA, in contrast, resulted in enhancement of the pyrene monomer emission with a decrease in the fluorescence band ratio. The extent of emission enhancement is dependent on the nucleobase adjacent to the U (pyr) in the pyrene oligomers. In one case, fluorescence increased 250-fold upon binding to complementary RNA. Other biological investigations included characterization of a mutant form of green fluorescent protein (GFP), which was shown to have a red-shifted fluorescence excitation spectrum and a higher fluorescence intensity than wild-type GFP (R3), covalent attachment of an extrinsic probe to GTP-binding protein for monitoring a GTP binding/GTPase cycle (R4), the use of diaminofluorescein dyes, which react with NO to yield the corresponding green fluorescent triazolofluoresceins, as fluorescent indicators for the detection of NO released from bovine aortic endothelial cells (ECs) (R5), and the use of a fluorogenic probe, N-acetyl-3,7dihydroxyphenoxazine (Amplex Red), in the enzymic detection of hydrogen peroxide (R6). A synthetic flavonol, 4′-N,N-dimethylamino-3-hydroxyflavone (DMA3HF), was investigated for use as a probe of model membranes (R7). The DMA3HF fluorophore exhibits both excited-state proton transfer and charge transfer. A covalent complex between bovine serum albumin and 7-hydroxycoumarin-4-acetic acid (BSA-HCA) was investigated as a probe of fatty acid concentration, based on quenching of the fluorescence emission upon association of fatty acids (FA) to the BSA-HCA complex (R8). Several papers described fluorescent probe systems for inorganic analysis. A functionalized ruthenium(II)-bis(terpyridine) complex was investigated as a luminescent sensor of zinc(II) (R9). The essentially nonfluorescent complex forms a luminescent rodlike 2:Zn2+:2 species. A series of tetraazatriphenylene derivatives was introduced as a new class of luminescence sensitizers with significant complexing power for lanthanide ions (R10). The 2:1 (ligand-ion) complexes exhibit high quantum yields for both Eu3+ and Tb3+. In a novel application, molecular fluorescence probes were used to trace the physical properties of heavy ion tracks such as dielectric constant of the probe’s surroundings and the molecular orientation of the probe molecules (R11). The orientation of the molecular probes was examined by use of polarized fluorescence spectroscopy. OTHER TECHNIQUES AND APPLICATIONS Several miscellaneous luminescence applications in biologically related areas were reported. A tissue site-selective terbium complex probe for tissue spectroscopy and endoscopy was used for in vitro, spatial, remote, quantitative imaging of the rat small intestine (S1). The probe preferentially binds to the inner surface of the small intestine and can be detected down to femtomole amounts. A study of the autofluorescence of dental caries revealed

characteristic emission of endogenous fluorophores with strong fluorescence bands in the red spectral region that do not appear in the spectra of healthy hard dental tissue (S2). The fluorescence spectra of the lesions were consistent with those of fluorescent porphyrins, mainly protoporphyrin IX, and may originate from bacterial biosynthesis in carious tissue. Delayed fluorescence excitation spectroscopy was used to study the phytoplankton composition of freshwaters and sediments and the algal composition of the benthos (S3). Delayed fluorescence is a measure of photosynthetic activity in living cells and can be used to distinguish between photosynthesis of green algae, diatoms, bluegreen algae, and cryptophytes. In an environmental application, fluorescence was used to investigate the origin of PAH compounds participating in the flotation processes of the Baltic Sea coastal zone (S4). Comparison among spectra of PAH in seawater, river water, the sea surface microlayer, sediments, suspended matter, and aerosols showed that the sediments of the Baltic Sea coastal zone in stormy weather are the main source of PAH contamination in the atmosphere. Another study (S5) looked at the fluorescence excitation and emission spectra of various woods in samples that included solid wood blocks, powder, and their extacts in MeOH. An instrument for routine analysis of the optically stimulated luminescence signal from single grains of sand was described (S6). Fluorescence was used to study the local microenvironment surrounding pyrene in several supercritical components of aviation fuels (n-pentane, n-hexane, n-heptane, n-octane) (S7). The results are fully consistent with observations for pyrene in other supercritical fluids such as CO2 and H2O. The maximum relative local density augmentation increases with increasing alkane chain length and correlates with changes in alkane polarizability. Elsewhere, fluorescence lifetime measurement of the intramolecular excimer-forming probe 1,3-bis(1′-pyrenyl)propane formed the basis of a liquid-phase thermometric method for determination of local temperatures of ethanol, dodecane, and Jet-A [hydrocarbon fuel (S8). The method is shown to be insensitive to the time- and/ or temperature-varying background fluorescence. Several other applications were described. The method of histograms was applied to results of fluorescence correlation spectroscopy to determine the polydispersity of particles and molecules in solution (S9). Laser-induced fluorescence emission spectroscopy of was used to probe electrospray plumes through measurement of fluorescent dyes in the spray stream (S10). Eosin Y was used to evaluate the sensitivity and reproducibility under typical electrospray conditions, and C.SNARF-1, a pH-sensitive dye, was used to monitor spray-induced pH changes within the electrospray plume. Luminescence spectroscopy was used to map the strain along fibers in model epoxy composites during tensile loading of the matrixes (S11), in a study of the micromechanics of fiber fragmentation. In the area of single-molecule detection, a multiplex technique was reported for identification of single fluorescent molecules in a flowing sample stream by correlated measurement of singlemolecule fluorescence burst size and intraburst fluorescence decay rate (S12). The technique was demonstrated for a dilute mixture of rhodamine 6G and tetramethylrhodamine isothiocyanate. Analytical Chemistry, Vol. 72, No. 12, June 15, 2000

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Philip B. Oldham is a professor of analytical chemistry and head of the Department of Chemistry at Mississippi State University. He received his B.S. in chemistry from Freed-Hardeman University in Henderson, TN, in 1980 and his Ph.D. in analytical chemistry from Texas A&M University in 1985 and joined the faculty at Mississippi State University in 1986. He currently serves on the editorial boards of the Microchemical Jounal and the International Journal of Bio-Chromatography. Dr. Oldham’s research interests involve the development of techniques for the characterization of solute molecules resident in specific microenvironments such as biological membranes, micelles, and/or surface films. The current technique of interest is total internal reflection fluorescence with electrochemical control of the sensor surface. Much of his efforts are currently being directed toward application of TIRF in the design and microfabrication of novel biosensor devices. Matthew E. McCarroll received his B.A. and B.S. degrees in chemistry and interdisciplinary studies from Appalachian State University in Boone, NC, in 1994. He then pursued graduate studies at the University of Idaho under the direction of Professor Ray von Wandruszka, where he received his Ph.D. in 1998. He is currently a postdoctoral research associate in Professor Isiah M. Warner’s group in the Chemistry Department at Louisiana State University. In the fall of 2000, he will join the faculty of the Department of Chemistry and Biochemistry at Southern Illinois University Carbondale as an assistant professor. His research interests focus on applications of fluorescence spectroscopy to study phenomena in micellar and organized media. These include the study of phase behavior in micellar solutions of nonionic surfactants, studies of chiral and molecular recognition, and the development of fluorescence sensors. Linda B. McGown received her B. S. in chemistry from the State University of New York at Buffalo in 1975 and her Ph.D. in chemistry from the University of Washington in 1979. She joined the faculty at Duke University in 1987, where she currently holds the position of Professor of Chemistry. She currently serves on the editorial boards of Analytical Chemistry, Applied Spectroscopy, and the Journal of Fluorescence and Instrumentation Science and Technology. Dr. McGown’s current research interests include the exploration of new fluorescence lifetime techniques for the characterization and analysis of complex samples, on -the-fly fluorescence lifetime detection in chromatography, molecular probe studies of chiral selectivity and molecular recognition, new approaches to the characterization of heterogeneous assemblies, exploration of novel organized media and nanostructures for chemical analysis, and fluorescence lifetime resolution in chiroptical measurements. Isiah M. Warner is Philip W. West Professor of Analytical and Environmental Chemistry at Louisiana State University. He received his B.S. in chemistry from Southern University in Baton Rouge, LA, in 1968 and his Ph.D. from the University of Washington in 1977. He joined the faculty of Emory University in 1982 and, from 1987, he was Samuel Candler Dobbs Professor of Chemistry at Emory University before joining the faculty of LSU in 1992. His current research interests include (1) fluorescence spectroscopy, (2) guest/host interactions, (3) studies in organized media, (4) chromatography, (5) environmental chemistry, and (6) mathematical analyses and interpretation of chemical data using chemometrics (chemical data analysis techniques). He is co-editor with Professor Linda McGown of volumes I and II of a series on multidimensional luminescence. He is a member of the American Chemical Society, Society for Applied Spectroscopy, American Association for the Advancement of Science, National Organization of Black Chemists, and Chemical Engineers, and Sigma Xi.

LITERATURE CITED (A1) Warner, I. M.; Soper, S. A.; McGown, L. B. Anal. Chem. 1998, 70, 477R-494R. BOOKS, REVIEWS, AND CHAPTERS OF GENERAL INTEREST (B1) Lakowicz, J. R. Principles of Fluorescence Spectroscopy, 2nd ed.; Kluwer Academic /Plenum: New York, 1999. (B2) Lakowicz, J. R., Ed. Topics in Fluorescence Spectroscopy: Nonlinear and Two-Photon-Induced Fluorescence; Plenum: New York, 1997; Vol. 5. (B3) Kettling, U.; Koltermann, A.; Schwille, P.; Eigen, M. Proc. Natl. Acad. Sci. U.S.A. 1998, 95 (4), 1416-1420. (B4) Koltermann, A.; Kettling, U.; Bieschke, J.; Winkler, T.; Eigen, M. Proc. Natl. Acad. Sci. U.S.A. 1998, 95 (4), 1421-1426. (B5) Lakowicz, J., Gryczynski, I. In Topics of Fluorescence Spectroscopy: Nonlinear and Two-Photon-Induced Fluorescence; Lakowicz, J. R., Ed.; Plenum: New York, 1997; Vol. 5, pp 87-144. (B6) Weiss, S. Science 1999, 282 (5408), 1676-1683. (B7) Wagnieres, G.; Star, W.; Wilson, B. Photochem. Photobiol. 1998, 68 (5) 603-632. (B8) Middendorf, L.; Amen, J.; Bruce, R.; Draney, D.; DeGraff, D.; Gewecke, J.; Grone, D.; Humprey, P.; Little, G.; Lugade, A.; Naryanan, N.; Oommen, A.; Osterman, H.; Peterson, R.; Rada, J.; Raghavachari, R.; Roemer, S., NATO ASI Ser., Ser. 3 1998, 52, 21-53. (B9) Silverman, L.; Campbell, R.; Broach, J., R. Curr. Opin. Chem. Biol. 1998, 2 (3), 397-403 206R


(B10) Auer, M.; Moore, K. J.; Meyer-Almes, F. J.; Guenther, R.; Pope, A. J.; Stoeckli, K. A. Drug Discovery Today 1998, 3 (10), 457465. (B11) Sittampalam, G.; Kahl, S.; Janzen, W. Curr. Opin. Chem. Biol. 1997, 1 (3), 384-391. (B12) Nickel, B. EPA Newsl. 1998, 64, 19-72. (B13) Schenk, G. Spectroscopy 1997, 12 (8), 48-52. (B14) Helms, M. Quimica 1998, 68, 17-21. (B15) Brennan, J. D. Appl. Spectrosc. 1999, 53 (3), 106A-121A. (B16) Olmstead, J. A.; Gray, D. G. Pulp Pap. Sci. 1997, 23 (12), J571-J581. (B17) Rao, T. P.; Reddy, M. L. P.; Pillai, A. R. Talanta 1998, 45 (5), 765-813. (B18) Kubista, M.; Nygren, J.; Elbergali, A.; Sjoback, R. Crit. Rev. Anal. Chem. 1999, 29 (1), 1-28. (B19) Sun, L.; Kantrowitz, E. R.; Galley, W. C. Proc. SPIE-Int. Soc. Opt. Eng. 1998, 3256, 236-242 (Advances in Optical Biophysics). (B20) Potyrailo, R. A., Hobbs, S. E., Hieftje, G. M. Fresenius J. Anal. Chem., 1998, 362 (4), 349-373. GENERAL INSTRUMENTAION (C1) Zwinkels, J. C.; Gauthier, F. Anal. Chim. Acta 1999, 380 (23), 193-209. (C2) Gardecki, J. A.; Maroncelli, M. Appl. Spectrosc. 1998, 52 (9), 1179-1189. (C3) Langhals, H.; Karolin, J.; Johansson, L. B. J. Chem. Soc., Faraday Trans. 1998, 94 (19), 2919-2922. (C4) Kotelevskiy, S. I. J. Lumin. 1998, 79 (3), 211-214. (C5) Credi, A.; Prodi, L. Spectrochim. Acta, Part A 1998, 54A (1), 159-170. (C6) Itami, S.; Araki, T. Proc. SPIE-Int. Soc. Opt. Eng. 1999, 3740, 408-411. (C7) Schmidt, W. J. Near Infrared Spectrosc. 1998, 6 (1-4), A159A162. (C8) Holst, G.; Kohls, O.; Klimant, I.; Konig, B.; Kuhl, M.; Richter, T. Sens. Actuators 1998, B, B51 (1-3), 163-170. (C9) Bogdanov, V.; Rogers, Y.-H.; Lan, G.; Boyce-Jacino, M. Proc. SPIE-Int. Soc. Opt. Eng. 1998, 3259, 156-164. (C10) Ratner, V.; Haas, E. Rev. Sci. Instrum. 1998, 69 (5), 21472154. (C11) Tupy, M. J.; Blanch, H. W.; Radke, C. J. Ind. Eng. Chem. Res. 1998, 37 (8), 3159-3168. (C12) Shimosaka, T.; Kitamori, T.; Harata, A.; Sawada, T. Appl. Spectrosc. 1998, 52 (2), 308-311. (C13) Barbini, R.; Colao, F.; Fantoni, R.; Palucci, A.; Ribezzo, S. Proc. SPIE-Int. Soc. Opt. Eng. 1999, 3534, 359-369. (C14) Committee, Analytical Methods (The Royal Society of Chemistry, London, W1V 0BN, U.K.). Analyst 1998, 123 (7), 16491656. (C15) Kao, S.; Asanov, A. N.; Oldham, P. B. Instrum. Sci. Technol. 1998, 26 (4), 375-387. (C16) Naqvi, K. R. Spectrosc. Lett. 1998, 31 (1), 147-155. (C17) Enderlein, J.; Kollner, M. Bioimaging 1998, 6 (1), 3-13. LASER-BASED TECHNIQUES (D1) Visser, A. J. W. G.; Hink, M. A. J. Fluoresc. 1999, 9 (1), 8187. (D2) Hansen, R. L.; Zhu, X. R.; Harris, J. M. Anal. Chem. 1998, 70, 1281-1287. (D3) Hattori, M.; Shimizu, H. Proc. SPIE-Int. Soc. Opt. Eng. 1999, 3602, 102-110. (D4) Chen, Y.; Muller, J. D.; So, P. T. C.; Gratton, E. Biophys. J. 1999, 77 (1), 553-567. (D5) Lakowicz, J. R.; Gryczynski, I.; Nowaczyk, K. Spectrochim. Acta, Part A 1997, 53A (10), 1637-1644. (D6) Volkmer, A.; Wynne, K.; Birch, D. J. S. Chem. Phys. Lett. 1999, 299 (5), 395-402. (D7) Sonnleitner, M.; Schutz, G. J.; Schmidt, T. Chem. Phys. Lett. 1999, 300 (1, 2), 221-226. (D8) Lohmannsroben, H.-G.; Roch, T.; Schultze, R. H. Polycyclic Aromat. Compd. 1999, 13 (2), 165-174. (D9) Rudnick, S. M.; Chen, R. F. Talanta 1998, 47 (4), 907-919. (D10) Ha, T.; Ting, A.; Liang, J.; Glass, J.; Chemla, D.; Schultz, P.; Weiss, S. Proc. SPIE-Int. Soc. Opt. Eng. 1998, 3273, 179185. (D11) Larsen, O. F. A.; Kozin, I. S.; Rijs, A. M.; Stroomberg, G. J.; de Knecht, J. A.; Velthorst, N. H.; Gooijer, C. Anal. Chem. 1998, 70 (6), 1182-1185. SENSORS (E1) Manyam, U. H.; Shahriari, M. R.; Morris, M. J. Proc. SPIE-Int. Soc. Opt. Eng. 1999, 3540, 10-18. (E2) Asundi, A. K.; Chen, J. W.; He, D. M. Proc. SPIE-Int. Soc. Opt. Eng. 1999, 3740, 561-564. (E3) Lo, L.-W.; Vinogradov, S. A.; Koch, C. J.; Wilson, D. F. Adv. Exp. Med. Biol. 1997, 428, 651-656. (E4) Amao, Y.; Asai, K.; Okura, I. Chem. Lett. 1999, 2, 183-184. (E5) Krause, C.; Werner, T.; Huber, C.; Klimant, I.; Wolfbeis, O. S. Anal. Chem. 1998, 70 (18), 3983-3985.

(E6) Blue, R.; Uttamchandani, D.; Wilson, C. G. IEE Proc.: Sci., Meas. Technol. 1999, 146 (1), 41-46. (E7) Roubani-Kalantzopoulou, F.; Kompitsas, M.; Mavropoulos, A.; Bassiotis, I. Proc. SPIE-Int. Soc. Opt. Eng. 1998, 3423, 266270. (E8) Moser-Boroumand, F.; Martins, J. M.; Fueri, P.; Forrer, M.; Mermoud, A.; Van den Bergh, H. Int. J. Environ. Anal. Chem. 1997, 68 (2), 239-256. (E9) Meusel, M.; Trau, D.; Katerkamp, A.; Meier, F.; Polzius, R.; Cammann, K. Sens. Actuators, B 1998, B51 (1-3), 249-255. (E10) Asanov, A. N.; Wilson, W. W.; Oldham, P. B. Anal. Chem. 1998, 70 (6), 1156-1163. SAMPLE PREPARATION, QUENCHING, AND RELATED PHENOMENA (F1) Goodpaster, J. V.; McGuffin, V. L. Appl. Spectrosc. 1999, 53 (8), 1000-1008. (F2) Ayala, J. H.; Afonso, A. M.; Gonzalez-Diaz, V. Microchem. J. 1998, 60 (2), 101-109. (F3) Gao, J.; Zhang, X.; Zhoa, B.; Yang, W.; Zhoa, Y.; Teng, X.; Kang, J. Anal. Lett. 1999, 32 (10), 2127-2139. (F4) Wilkinson, F.; Abdel-Shafi, A. A. J. Phys. Chem. A 1999, 103 (23), 5425-5435. (F5) Cioni, P.; Strambini, G. B. J. Am. Chem. Soc. 1998, 120 (45), 11749-11757. (F6) Nygren, J.; Elbergali, A.; Kubista, M. Anal. Chem. 1998, 70 (22), 4841-4846. (F7) Potyrailo, R. A.; Hieftje, G. M. Anal. Chim. Acta 1998, 370 (1), 1-8. DATA REDUCTION (G1) Suarez Araujo, C. P. Biomed. Chromatogr. 1999, 13 (2), 187188. (G2) Todeschini, R.; Galvangi, D. TrAC, Trends Anal. Chem. 1999, 18 (2), 93-98. (G3) Ferrer, R.; Guiteras, J.; Beltran, J. L. Anal. Chim. Acta, 1999, 384 (3), 261-269. (G4) Munck, L.; Norgaard, L.; Engelsen, S. B.; Bro, R.; Andersson, C. A. Chemom. Intell. Lab. Syst, 1998, 44 (1, 2), 31-60. (G5) Bro, R. Chemom. Intell. Lab. Syst. 1999, 46 (2), 133-147. (G6) Prakash, A. M. C.; Stellman, C. M.; Booksh, K. S. Chemom. Intell. Lab. Syst. 1999, 46 (2), 265-274. (G7) Dufour, E.; Riaublanc, A. Lait 1997, 77 (6), 657-670. (G8) Villegas, M. M.; Neal, S. L. J. Phys. Chem. 1997, 101, 68906896. LUMINESCENCE IN ORGANIZED MEDIA (H1) Garg, B. S.; Bhojak, N.; Bist, J. S.; Singh, G. K., Indian J. Chem., Sect. A: Inorg., Bio-inorg., Phys., Theor. Anal. Chem., 1999, 38A (4), 392-394. (H2) Wang, Z.-P.; Qian, Y.-H.; Chen, G.-S.; Cheng, K L. Microchem. J. 1998, 60 (3), 271-281. (H3) Pandey, S.; Acree, W., E., Jr; Fetzer, J. C. Talanta 1998, 47 (3), 769-778. (H4) Romanovskaya, G. I.; Koroleva, M. V.; Blinov, A. N.; Zuev, B. K. J. Anal. Chem. 1999, 54 (7), 623-626. (H5) Hagestuen, E. D.; Campiglia, A. D. Talanta 1999, 49 (3), 547560. (H6) Rawatt, S. S.; Chattopadhyay, A. J. Fluoresc. 1999, 9 (3), 233244. (H7) McCarroll, M.; Toerne, K.; von Wandruszka, R. Langmuir 1998, 14 (11), 2965-2969. (H8) McCarroll, M.; Toerne, K.; von Wandruszka, R. Langmuir 1998, 14 (21), 6096-6100. (H9) McCarroll, M. E.; Joly, A. G.; Wang, Z. M.; Friedrich D. M.; von Wandruszka, R. J. Colloid Interface Sci. 1999, 218 (1), 260-264. (H10) Billiot, E.; Agbaria, R, A,; Thibodeaux, S,; Shamsi, S,; Warner I. M. Anal. Chem. 1999, 71 (7), 1252-1256. (H11) Roberts, E. L.; Burguieres, S.; Warner, I. M. Appl. Spectrosc. 1998, 52 (10), 1305-1313. (H12) Lee, S, S.; Kiserow, D. J.; McGown, L. B. J. Colloid Interface Sci. 1997, 193 (1), 32-40. (H13) Polewski, K.; Napierala, D. Carbohydr. Res. 1999, 315 (1-2), 35-47. (H14) Munoz, J. A.; Campana, A. M.; Barero, F. A. Talanta 1998, 47 (2), 387-399. (H15) Villegas, M. M.; Neal, S. L. J. Phys. Chem. 1997, 101, 68906896. (H16) Pistolis, G. Chem. Phys. Lett. 1999, 304 (5, 6), 371-377. (H17) Escandar, G. M. Analyst (Cambridge, U. K.) 1999, 124 (4), 587-591. (H18) Liu, Z.; Cai, R.; Mao, L.; Huan, H.; Ma, W. Analyst (Cambridge, U. K.) 1999, 124 (2), 173-176. (H19) Datta, A.; Mandal, D.; Kumar P. S.; Das, S.; Bhattacharyya, K. J. Chem. Soc. 1998, 94 (23), 3471-3475. (H20) Cui, H.; Zhang, H.; Xi, S.; Wang, R. J. Mater. Sci. Lett. 1998, 17 (11), 913-915. (H21) Manjula, A.; Nagarajan, M. Indian J. Chem., Sect. B: Org. Chem. Incl. Med. Chem. 1998, 37B (6), 527-535.

(H22) Dey, J.; Roberts, E. L.; Warner I. M. J. Phys. Chem. A 1998, 102 (1), 301-305. (H23) Delmarr, D.; Veret-Lemarinier, A.; Bied-Charreton, C. J. Lumin. 1999, 82 (1), 57-67. (H24) Hartnett, A. M.; Ingersoll, C. M.; Baker, G. A.; Bright, F. V. Anal. Chem. 1999, 71 (6), 1215-1224. (H25) Yan, Y.; Myrick, M. L. Anal. Chem. 1999, 71 (10), 19581962. (H26) Zhang, Y.; Pham, T. H.; Sanchez Pena, M.; Agbaria, R. A.; Warner, I. M. Appl. Spectrosc. 1998, 52 (7), 952-957. (H27) Zhang, Y. L.; Agbaria, R. A.; Warner, I. M. Supramol. Chem. 1997, 8 (4), 309-318. (H28) Grady, T.; Joyce, T.; Smyth, M. R.; Diamond, D.; Harris, S. J. Anal. Commun. 1998, 35 (4), 123-125. (H29) Engebretson, R. B.; von Wandruszka, R. Environ. Sci. Technol. 1998, 32 (4), 488-493. (H30) Sharpless, C. M.; McGown, L. B. Environ. Sci. Technol. 1999, 33 (18), 3264-3270. (H31) von Wandruszka, R. Soil Sci. 1998, 163 (12), 921-930. LOW-TEMPERATURE LUMINESCENCE (I1) Belykh, L. I.; Kireeva, A. N.; Smagunova, A. N.; Penzina, E. E.; Pan'kov, S. D.; Protasova, L. E. J. Anal. Chem. 1999 54 (7), 596-602. (I2) Ollikainen, O.; Palm, V.; Rebane, K. Proc. Est. Acad. Sci. 1997 46 (4), 273-280. (I3) Caspary, N.; Palm, V.; Rebane, K. K.; Bondybey, V. E. Chem. Phys. Lett. 1998 283 (5, 6), 345-349. TOTAL LUMINESCENCE AND SYNCHRONOUS EXCITATION SPECTROSCOPIES AND RELATED TECHNIQUES (J1) Li, Y.-Q.; Huang, X.-Z.; Xu, J.-G. J. Fluoresc. 1999, 9 (3), 173179. (J2) Hyfantis, G. J., Jr.; Watts, W.; Finnegan, T. P. Proc. SPIE-Int. Soc. Opt. Eng. 1999, 3534, 92-99. (J3) Fang, F.; Kanan, S.; Patterson, H. H.; Cronan, C. S. Anal. Chim. Acta 1998, 373 (2-3), 139-151. (J4) Blaser, P.; Heim, A.; Luster, J. Environ. Int. 1999, 25 (2/3), 285-293. (J5) Smith, D. S.; Kramer, J. R. Anal. Chim. Acta 1998, 363 (1), 21-29. (J6) Ruiz, T. P.; Lozano, C. M.; Tomas, V.; Carpena, J. Talanta 1998, 47 (3), 537-545. (J7) Murillo Pulgarin, J. A.; Alanon Molina, A.; Fernandez Lopez, P. Anal. Chim. Acta 1998, 370 (1), 9-18. (J8) Berzas Nevado, J. J.; Gomez Laguna, M. A.; Murillo Pulgarin, J. A.; Amador-Hernandez, J.; Gomez Laguna, M. A. Analyst 1997, 123 (3), 483-488. (J9) Sabry, S. M. Anal. Chim. Acta 1997, 351 (1-3), 211-221. (J10) Ferrer, R.; Beltran, J. L.; Guiteras, J. Talanta 1998, 45 (6), 1073-1080. (J11) Ayala, J. H.; Afonso, A. M.; Diaz, V. G. J. Fluoresc. 1997, 7 (2), 147-153. (J12) Roch, T. Anal. Chim. Acta 1997, 356 (1), 61-74. (J13) Marose, S.; Lindemann, C.; Scheper, T. Biotechnol. Prog. 1998, 14 (1), 63-74. (J14) Lindemann, C.; Marose, S.; Nielsen, H. O.; Scheper, T. Sens. Actuators, B 1998, B51 (1-3), 273-277. (J15) Lindemann, C.; Marose, S.; Scheper, T.; Nielsen, H. O.; Hitzmann, B.; Belgardt, K.-H. Proc. SPIE-Int. Soc. Opt. Eng. 1999, 3534, 83-90. (J16) Gray, P. C.; Shokair, I. R.; Rosenthal, S. E.; Tisone, G. C.; Wagner, J. S.; Rigdon, L. D.; Siragusa, G. R.; Heinen, R. J. Appl. Opt. 1998, 37 (25), 6037-6041. (J17) Chen, Z.; Liu, Q.; Wang, S.; Xu, X.; Yu, H. Spectrochim. Acta, Part A 1999, 55A (9), 1909-1914. (J18) Yang, X.; Ju, C.; Sun, G.; Yang, H.; Lu, T. Microchem. J. 1998, 60 (3), 210-216. SOLID SURFACE LUMINESCENCE (K1) Zandomeneghi, M. J. Agric. Food Chem. 1999, 47 (3), 878882. (K2) Dufour, E.; Riaublanc, A. Lait 1997, 77 (6), 657-670. (K3) Billa, E.; Koutsoula, E.; Koukios, E. G., Bioresour. Technol. 1999, 67 (1), 25-33. (K4) Capitan-Vallvey, L. F.; Deheidel, M. K.; Avidad, R. Mikrochim. Acta 1999, 130 (4), 273-279. (K5) Capitan-Vallvey, L. F.; Deheidel, M. K. A.; de Orbe, I.; Avidad, R. Analyst 1999, 124 (1), 49-53. (K6) Campiglia, A. D.; Vo-Dinh, T. Anal. Chim. Acta 1998, 372 (3), 349-355. (K7) Kitade, T.; Kitamura, K.; Wada, Y. Anal. Chim. Acta 1998, 36(1-3), 33-39. (K8) Alava-Moreno, F.; Valencia-Gonzalez, M. J.; Diaz-Garcia, M. E. Analyst 1998, 123 (4), 691-694. (K9) Tjioe, S. W.; Hurtubise, R. J. Appl. Spectrosc. 1998, 52 (3), 414-419. (K10) Li, M.; Hurtubise, R. J. Anal. Lett. 1998, 31 (3), 491-510.


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(K11) Li, M.; Hurtubise, R. J.; Weston, A. Anal. Chem. 1999, 71 (20), 4679-4683. (K12) Chen, J.; Hurtubise, R. J. Talanta 1998, 45 (6), 1081-1087. (K13) Ackerman, A. H.; Hurtubise, R. J. Appl. Spectrosc. 1999, 53 (7), 770-775. (K14) Ramasamy, S. M.; Hurtubise, R. J. Talanta 1998, 47 (4), 971979 LUMINESCENCE IN CHROMATOGRAPHY, ELECTROPHORESIS, AND FLOW SYSTEMS (L1) Weinmann, Angela R. M.; Oliveria, Marcio S.; Jorge, Salim M.; Martins, Antonio R. J. Chromatogr., B: Biomed. Sci. Appl. 1999, 729 (1+2), 231-236. (L2) Lechowicx, Wojciech, Z. Zagadnien Nauk Sadowych 1999, 39, 54-64. (L3) Beltran, J. L.; Guiteras, J.; Ferrer, R. Anal. Chem. 1998, 70 (9), 1949-1955. (L4) Moutiez, E.; Prognon, P.; Bourrinet, P.; Zehaf, S.; Dencausse, A.; Manhuzier, G. Analyst (Cambridge, U. K.) 1997, 122 (11), 1347-1352. (L5) Bueldt, A.; Karst, U. Anal. Chem. 1999, 71 (15), 3003-3007. (L6) Benito, I.; Marina, M. L.; Saz, J. M.; Diez-Masa, J. C. J. Chromatogr., A 1999, 841 (1), 105-114. (L7) Van Orden, A.; Keller, R. A. Anal. Chem. 1998, 70 (21), 44634471. (L8) Fuller, R. R.; Moroz, L. L.; Gillette, R.; Sweedler, J. V. Neuron 1998, 20 (2), 173-181. (L9) Fultz, A.; Branch, T. M.; Majidi, V. Microchem. J. 1997, 57 (2), 231-244. (L10) Shamsi, S. A.; Danielson, N. D.; Warner, I. M. J. Chromatgr., A 1999, 835 (1-2), 159-168. (L11) He H, Nunnally B. K.; Li, L. C.; McGown, L. B. Anal. Chem. 1998, 70 (16), 3413-3418. (L12) Li, L. J.; McGown, L. B. J. Chromatgr., A 1999, 841 (1), 95103. (L13) Hoch, R. L. Analyst (Cambridge, U. K.) 1999, 124 (5), 793796. (L14) Ensafi, A. A.; Rezaei, B. Microchem. J. 1998, 60 (1), 75-83. (L15) Perez-Ruiz, T.; Martinez-Lozano, C.; Tomas, V.; Fenoll, J. Analyst (Cambridge, U. K.) 1998, 123 (7), 1577-1581. (L16) Smith, R. M.; Chienthavorn, O.; Danks, N.; Wilson, I. D. J. Chromatogr., A 1998, 798 (1+2), 203-206. DYNAMIC MEASUREMENTS OF LUMINESCENCE (M1) Berezhkovskii, A. M.; Szabo, A.; Weiss, G. H. J. Chem. Phys. 1999, 110 (18), 9145-9150. (M2) Golub, A. S.; Popel, A. S.; Zheng, L.; Pittman, R. N. Photochem. Photobiol. 1999, 69 (6), 624-632. (M3) D'Alfonso, L.; Collini, M.; Baldini, G. Biochim. Biophys. Acta 1999, 1432 (2), 194-202. (M4) Clayton, A. H. A.; Sawyer, W. H. Biophys. J. 1999, 76 (6), 3235-3242. (M5) Visser, A. J. W. G.; van den Berg, P. A. W.; Visser, N. V.; van Hoek, A.; van den Burg, H. A.; Parsonage, D.; Claiborne, A. J. Phys. Chem. B 1998, 102 (50), 10431-10439. (M6) Gaft, M.; Reisfeld, R.; Panczer, G.; Blank, Ph.; Boulon, G. Spectrochim. Acta, Part B 1998, 53B (13), 2163-2175. (M7) Gottschlich, S.; Lippert, B. M.; Schade, W.; Werner, J. A. Res. Commun. Mol. Pathol. Pharmacol. 1997, 98 (2), 237-240. FLUORESCENCE POLORIZATION, MOLECULAR DYNAMICS, AND RELATED PHENOMENA (N1) Ha, T.; Laurence, T. A.; Chemla, D. S.; Weiss, S. J. Phys. Chem. B 1999, 103 (33), 6839-6850. (N2) Ha, T.; Ting, A. Y.; Liang, J.; Caldwell, W. B.; Deniz, A. A.; Chemla, D. S.; Schultz, P. G.; Weiss, S. Proc. Natl. Acad. Sci. 1999, 96 (3), 893-898. (N3) Bilsel, O.; Yang, L.; Zitzewitz, J. A.; Beechem, J. M.; Matthews, C. R. Biochemistry 1999, 38 (13), 4177-4187. (N4) Chakrabarti, A.; Bera, A. K.; Das, B.; Chattopadhyay, S.; Sarkar, D.; DasGupta, C. Curr. Sci. 1999, 76 (9), 1235-1238. (N5) Chandy, I. K.; Lo, J.; Ludescher; R. D. Biochemistry 1999, 38 (29), 9286-9294. (N6) Ishizaka, S.; Habuchi, S.; Kim, H.; Kitamura, N. Anal. Chem. 1999, 71 (16), 3382-3389. (N7) Hink, M. A.; van Hoek, A.; Visser, A. J. W. G. Langmuir 1999, 15 (4), 992-997. CHEMILUMINESCENCE (O1) Cherednikova, E. Yu.; Chikishev, A. Yu.; Dement′eva, E. I.; Kosobokova, O. V. Proc. SPIE-Int. Soc. Opt. Eng. 1999, 3732, 214-219. (O2) Arakawa, H.; Tsuji, A.; Maeda, M. J. Biolumin. Chemilumin. 1998, 13 (6), 349-354. (O3) Kuroda, N.; Hosoki, S.; Nakashima, K.; Akiyama, S.; Givens, Richard S. J. Biolumin. Chemilumin, 1998, 13 (2), 101-105. 208R


(O4) Traykov, T.; Hadjimitova, V.; Goliysky, P.; Ribarov, S. Gen. Physiol. Biophys. 1997, 16 (1), 3-14. NEAR-INFRARED FLUORESCENCE (P1) Kukrer, B.; Akkaya, E. U. Tetrahedron Lett. 1999, 40 (51), 9125-9128. (P2) Gallaher, D. L., Jr.; Johnson, M. E. Analyst 1999, 124 (11), 1541-1546. (P3) Baars, M. J.; Patonay, G. Anal. Chem. 1999, 71, 1 (3), 667671. (P4) Tung, C.-H.; Bredow, S.; Mahmood, U.; Weissleder, R. Bioconjugate Chem. 1999, 10 (5), 892-896. (P5) Hofstraat, J. W.; Wolbers, M. P. Oude; Van Veggel, F. C. J. M.; Reinhoudt, D. N.; Werts, M. H. V.; Verhoeven, J. W. J. Fluoresc. 1998, 8 (4), 301-308. (P6) Tarazi, L.; George, A.; Patonay, G.; Strekowski, L. Talanta 1998, 46 (6), 1413-1424. (P7) Hanlon, E. B.; Itzkan, I.; Dasari, R. R.; Feld, M. S.; Ferrante, R. J.; McKee, A. C.; Lathi, D.; Kowall, N. W., Photochem. Photobiol. 1999, 70 (2), 236-242. (P8) Flanagan, J. H., Jr.; Owens, C. V.; Romero, S. E.; Waddell, E.; Kahn, S. H.; Hammer, R. P.; Soper, S. A. Anal. Chem. 1998, 70 (13), 2676-2684. (P9) Soper, S. A.; Ford, S. M.; Xu, Y.; Qi, S.; McWhorter, S.; Lassiter, S.; Patterson, D.; Bruch, R. C. J. Chromatogr., A 1999, 853 (1 + 2), 107-120. (P10) Middendorf, L.; Amen, J.; Bruce, R.; Draney, D.; DeGraff, D.; Gewecke, J.; Grone, D.; Humphrey, P.; Little, G.; Lugade, A.; Narayanan, N.; Oommen, A.; Osterman, H.; Peterson, R.; Rada, J.; Raghavachari, R.; Roemer, S. NATO ASI Ser., Ser. 3 1998, 52, 21-53. (P11) Zhang, Y.; Soper, S. A.; Middendorf, L. R.; Wurm, J. A.; Erdmann, R.; Wahl, M. Appl. Spectrosc. 1999, 53 (5), 497504. (P12) Waddell, E.; Stryjewski, W. J.; Soper, S. A. Rev. Sci. Instrum. 1999, 70 (1, Pt. 1), 32-37. (P13) Daneshvar, M. I.; Peralta, J. M.; Casay, G. A.; Narayanan, N.; Evans, Lawrence, III.; Patonay, G. J. Immunol. Methods 1999, 226 (1-2), 119-128. (P14) Baars, M. J.; Patonay, G. Appl. Spectrosc. 1998, 52 (12), 16191622. LUMINESCENCE TECHNIQUES IN BIOLOGICAL AND CLINICAL ANALYSIS (Q1) Gradl, G.; Guenther, R.; Sterrer, S. BioMethods (Basel), 10, 1999, 331-351 (Microsystem Technology: A Powerful Tool for Biomolecular Studies). (Q2) Haupts, U.; Maiti, S.; Schwille, P.; Webb, W. W. Proc. Natl. Acad. Sci. U.S.A. 1998, 95 (23), 13573-13578. (Q3) Chattopadhyay, A.; Mukherjee, S. Langmuir 1999, 15 (6), 2142-2148. (Q4) Schmid, E. L.; Tairi, A.; Hovius, R.; Vogel, H. Anal. Chem. 1998, 70 (7), 1331-1338. (Q5) De Rossi, U.; Hermel, H. Appl. Spectrosc. 1999, 53 (5), 505509. (Q6) Griffin, B. A.; Adams, S. R.; Tsein, R. Y. Science 1998, 281 (5374), 269-272. (Q7) Windsor, S. A.; Tinker, M. H.; Osborne, M. R.; Seidel, A. Inst. Phys. Conf. Ser. 1996, 150, 321-326. (Q8) Holeman, L. A.; Robinson, S. L.; Szostak, J. W.; Wilson, C. Folding Des. 1998, 3 (6), 423-431. (Q9) Abramo, K. H.; Pitner, J. B.; McGown, L. B. Biospectroscopy 1998, 4 (1), 27-35. (Q10) Bonnet, G.; Krichevsky, O.; Libchaber, A. Proc. Natl. Acad. Sci. U.S.A. 1998, 95 (15), 8602-8606. (Q11) Hakala, H.; Virta, P.; Salo, H.; Lonnberg, H. Nucleic Acids Res. 1998, 26 (24), 5581-5588. (Q12) Li, W.; Lu, H.; Xu, C.; Zhang, J.; Lu, Z. Spectrosc. Lett. 1998, 31 (6), 1287-1298. (Q13) Gong, G.; Zong, Z.; Song, Y. Spectrochim. Acta, Part A 1999, 55A (9), 1903-1907. (Q14) Winkler, T.; Kettling, U.; Koltermann, A.; Eigen, M. Proc. Natl. Acad. Sci. U.S.A. 1999, 96 (4), 1375-1378. (Q15) Garcia S., F.; Navas Diaz, A.; Gonzalez Diaz, A. F.; Torijas, M. C.; Alcantara, D.; Eremin, S. A. Anal. Chim. Acta 1999, 395 (1-2), 133-142. (Q16) Rubenstein, R.; Gray, P. C.; Wehlburg, C. M.; Wagner, J. S.; Tisone, G. C., Biochem. Biophys. Res. Commun. 1998, 246 (1), 100-106. (Q17) Slobozhanina, E. I.; Kozlova, N. M.; Kas’ko, L. P.; Mamontova, M. V.; Chernitskii, E. A. J. Appl. Spectrosc. 1999, 65 (6), 988991. (Q18) Rosen, D. L. Rev. Anal. Chem. 1999, 18 (1-2), 1-21. (Q19) Pellegrino, P. M.; Fell, N. F., Jr.; Rosen, D. L.; Gillespie, J. B. Anal. Chem. 1998, 70 (9), 1755-1760. REAGENTS AND PROBES (R1) Pandey, R. K.; Tripathi, S.; Misra, K. Nucleosides Nucleotides 1998, 17 (9-11), 1937-1948.

(R2) Yamana, K.; Iwase, R.; Furutani, S.; Tsuchida, H.; Zako, H.; Yamaoka, T.; Murakami, A. Nucleic Acids Res. 1999, 27 (11), 2387-2392. (R3) Inouye, S.; Umesono, K.; Tsuji, F. I. Methods Enzymol. 1999, 302, 444-449. (R4) Nomanbhoy, T.; Cerione, R. A. Methods Mol. Biol. 1998, 84, 237-247. (R5) Nakatsubo, N.; Kojima, H.; Kikuchi, K.; Nagoshi, H.; Hirata, Y.; Maeda, D.; Imai, Y.; Irimura, T.; Nagano, T. FEBS Lett. 1998, 427 (2), 263-266. (R6) Zhou, M.; Diwu, Z.; Panchuk-Voloshina, N.; Haugland, R.P. Anal. Biochem. 1997, 253 (2), 162-168. (R7) Dennison, S. M.; Guharay, J.; Sengupta, P. K. Spectrochim. Acta, Part A 1999, 55A (5), 1127-1132. (R8) Demant, E. J. F. Anal. Biochem. 1999, 267 (2), 366-372. (R9) Barigelletti, F.; Flamigni, L.; Calogero, G.; Hammarstrom, L.; Sauvage, J.; Collin, J. Chem. Commun. 1998, 21, 2333-2334. (R10) van Der Tol, E. B.; van Ramesdonk, H. J.; Verhoeven, J. W.; Steemers, F. J.; Kerver, E. G.; Verboom, W.; Reinhoudt, D. N. Chem.- Eur. J. 1998, 4 (11), 2315-2323. (R11) Esser, M.; Fuhrmann, J. Radiat. Meas. 1999, 31 (1-6), 4550. OTHER TECHNIQUES AND APPLICATIONS (S1) Houlne, M. P.; Hubbard, D. S.; Kiefer, G. E.; Bornhop, D. J. J. Biomed. Opt. 1998, 3 (2), 145-153.

(S2) Konig, K.; Flemming, G.; Hibst, R. Cell. Mol. Biol. 1998, 44 (8), 1293-1300. (S3) Gerhardt, V.; Bodemer, U. Limnologica 1998, 28 (3), 313322. (S4) Spirkauskaite, N.; Tarasiuk, N.; Milukaite, A.; Petelski, T.; Chomka, M.; Lujanas, V. Environ. Phys. 1998, 20 (2), 50-54. (S5) Pandey, K. K.; Upreti, N. K.; Srinivasan, V. V. Wood Sci. Technol. 1998, 32 (4), 309-315. (S6) Duller, G. A. T.; Botter-Jensen, L.; Kohsiek, P.; Murray, A. S. Radiat. Prot. Dosim. 1999, 84, 325-330 (1-4, Solid State Dosimetry, Pt. 1). (S7) Niemeyer, E. D.; Bright, F. V. Energy Fuels 1998, 12 (4), 823827. (S8) Buckner, S. W.; Forlines, R. A.; Gord, J. R. Appl. Spectrosc. 1999, 53 (1), 115-122. (S9) Starchev, K.; Buffle, J.; Perez, E. J. Colloid Interface Sci. 1999, 213 (2), 479-487. (S10) Zhou, S.; Edwards, A. G.; Cook, K. D.; van Berkel, G. J. Anal. Chem. 1999, 71 (4), 769-776. (S11) Yallee, R. B.; Young, R. J. Composites, Part A 1998, 29A (11), 1353-1362. (S12) Van Orden, A.; Machara, N. P.; Goodwin, P. M.; Keller, R. A. Anal. Chem. 1998, 70 (7), 1444-1451.

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