Downloaded by 80.82.77.83 on March 26, 2018 | https://pubs.acs.org Publication Date: June 9, 1998 | doi: 10.1021/bk-1998-0692.pr001
Preface
I his volume is based on a symposium of the same title held at the San Francisco American Chemical Society meeting in April 1997. It brought together many of the major international researchers in the field of spectroscopy in bioinorganic chemistry. It was also designed to have a broad-based appeal to researchers in the fields of bioinorganic, physical-inorganic, inorganic, and biochemistry. This was accomplished through a significant tutorial component emphasizing recent advances in the key spectroscopic and related methods and through a series of sessions focusing on general topics in bioinorganic chemistry where spectroscopy has had a strong impact. The organization of this volume parallels the symposium. The first part (Recent Advances in Ground-State and in Excited-State Methods) emphasizes important new directions in the different methods of bioinorganic spectroscopy. Included with the ground-state methods is X-ray diffraction. Spectroscopy and protein crystallography strongly complement each other and through their combination one can maximize insight into the geometric and electronic structure of an active site and their contributions to function in biology. Also included with the excited-state spectroscopic methods is a contribution on electronic structure calculations. Spectroscopy probes the electronic structure of an active site and if calculations correlate well with data they can define specific bonding interactions that can activate a metal center for reactivity. The second part of this volume focuses on four areas of bioinorganic chemistry where spectroscopy has had a huge impact: electron transfer, cluster interactions, active site geometric and electronic structure, and intermediates. This list was limited only by the number of sessions available to the symposium. Contributors to each topic include both researchers who focus on the detailed application of specific spectroscopic methods and those who apply a range of methods to achieve insight into reactivity. Thus for example, in the electron transfer section contributions include both detailed resonance Raman and X-ray absorption spectroscopy of blue copper, iron sulfur, and the Cu center in cytochrome c oxidase and the use of absorption and resonance Raman spectroscopies to probe electron transfer induced protein folding in heme proteins. A
ix Solomon and Hodgson; Spectroscopic Methods in Bioinorganic Chemistry ACS Symposium Series; American Chemical Society: Washington, DC, 1998.
A few of the contributors to the symposium were not able to submit a manuscript within the time constraints for this volume and we suggest the reader go to the following references for the topic they covered in the symposium. "The Electron Structure of Cu : A Novel Mixed-Valence Dinuclear Copper ElectronTransfer Center", Farrar, Jacqui Α.; Neese, Frank; Lappalainen, P.; Kroneck, Peter M. H.; Sarraste, M.; Zumft, W. G.; Thomson, Andrew J. / Am. Chem. Soc. 1996, 118, 11501-11514. A
Downloaded by 80.82.77.83 on March 26, 2018 | https://pubs.acs.org Publication Date: June 9, 1998 | doi: 10.1021/bk-1998-0692.pr001
Stephens, Philip (Presenter) Two Ph.D. theses: "Azotobacter Vinelandii Ferredoxin I: Spectroscopic and Theoretical Studies," Jensen, G. M. 1995; "Spectroscopic Studies of Chemically and Mutated Forms of Azotobacter Vinelandii Ferredoxin I", Reyntjens, B. R. University of Southern California, Los Angeles, CA, 1996. "Molybdenum-Iron Sulfide-Bridged Double Cubanes", Huang, Jiesheng; Mukerjee, Subhashish; Segal, Brent M.; Akashi, Haruo; Zhou, Jian; Holm, R. H. /. Am. Chem. Soc. 1997,119, 8662-8674. "X-ray Absorption and EPR Studies on the Copper Ions Associated with the Particu late Methane Monooxygenase from Methylococcus capsulatus (Bath)", Nguyen, HiepHoa T.; Nakagawa, Kent H.; Hedman, Britt; Elliot, Sean J.; Lidstrom, Mary E.; Hodg son, Keith O.; and Chan, Sunney I. J. Am. Chem. Soc. 1996, 118, 12766-12776; "Regio- and Stereoselectivity of Particulate Methane Monooxygenase from Methylo coccus capsulatus (Bath)", Elliot, Sean J.; Zhu, Mei; Tso, Luke; Nguyen, H.-Hoa T.; Yip, John H.-K; Chan, Sunney I. J. Am. Chem. Soc. 1997,119, 9949-9955. "EXAFS Studies of FeMo-Cofactor and MoFe Protein: Direct Evidence for the Long Range Mo-Fe-Fe Interaction and Cyanide Binding to the Mo in FeMo-Cofactor," Liu, H. I.; Filipponi, Α.; Gavini, N.; Burgess, Β. K ; Hedman, B.; Di Cicco, Α.; Natoli, C. R.; Hodgson, K. O. /. Am. Chem. Soc. 1994,116, 2418-2423. "Heme/Copper Terminal Oxidases", Ferguson-Miller, S.; Babcock, G. T. Chem. Rev. 1996, 96 2889-2907; "Low-Powered Picosecond Resonance Raman Evidence for Histidine Ligation to Heme after Photodissociation of CO from Cytochrome c Oxidase", Schelvis, J. P. M.; Deinum, G.; Varotsis, C. Α.; Ferguson-Miller, S.; Babcock, G. T. J. Am. Chem. Soc. 1997,119, 8409-8416. Acknowledgments We want to thank the participants for their excellent and timely contributions to the field of bioinorganic chemistry. The symposium was made possible through the generous support of the U.S. Department of Energy Biological and Envi ronmental Research Program, which provided general support and student travel
χ Solomon and Hodgson; Spectroscopic Methods in Bioinorganic Chemistry ACS Symposium Series; American Chemical Society: Washington, DC, 1998.
awards. Additional funding was provided by the Inorganic Division of the American Chemical Society and by the Society of Biological Inorganic Chemistry. EDWARD I. SOLOMON
Department of Chemistry Stanford University Stanford, CA 94305
Downloaded by 80.82.77.83 on March 26, 2018 | https://pubs.acs.org Publication Date: June 9, 1998 | doi: 10.1021/bk-1998-0692.pr001
KEITH O . HODGSON
Department of Chemistry Stanford University Stanford, CA 94305
xi Solomon and Hodgson; Spectroscopic Methods in Bioinorganic Chemistry ACS Symposium Series; American Chemical Society: Washington, DC, 1998.
