Addition/Correction Cite This: Chem. Rev. XXXX, XXX, XXX−XXX
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Correction to Single-Molecule Fluorescence Spectroscopy of Photosynthetic Systems Toru Kondo, Wei Jia Chen, and Gabriela S. Schlau-Cohen* Chem. Rev. 2017, 117 (2), pp 860−898. DOI: 10.1021/acs.chemrev.6b00195
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of the protein energy landscape is shown (right). The multiple levels of barrier heights as a function of a generalized nuclear coordinate give rise to the so-called hierarchy of conformational substates, as well as conformational switching between these substates. This rugged, dynamic protein energy landscape combines with pigments to produce photosynthetic pigment−protein complexes (left). In these complexes, pigments are embedded within a surrounding protein scaffold, with just a few angstroms between the neighboring pigments and between the pigments and the surrounding protein. As a result, the conformational dynamics of the protein introduces dynamics into the electronic structure.
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he authors provide the following correction to Figure 4: in panel (b) in the original figure, the gray solar spectrum was incorrectly overlaid on the x-axis and the green Chl a spectrum was incorrect. These errors have been corrected in the revised version below.
Figure 4. Pigment−protein complexes are optimized by pigment selection, protein environment, and protein dynamics. (a) Common pigments in photosynthetic light harvesting are shown. The carotenoid beta-carotene (left, orange box) is abundant in plants, fruits, and vegetables. Carotenoid variants have a photoprotective role in many photosynthetic organisms. Chl a (center, green box) is found in higher plants, green algae, and some bacteria. Chls are circular tetrapyrroles, and Chl variants are the major light-harvesting pigment in these organisms. Phycocyanobilin (right, blue box) is a phycobilin pigment. Phycobilins are open tetrapyrroles that covalently bind to the protein structure. Phycobilin variants are the light-harvesting pigments in cyanobacteria, red algae, and cryptophytes. (b) Photosynthetic systems achieve broad solar coverage (gray line) through this set of pigments (orange, green, and blue lines indicate absorption spectra of carotenoid, Chl a, and phycocyanin, respectively), with further spectral tuning by different substituent groups to generate other pigment variants and by electrochromic shifts induced by the protein-binding pocket. (c) A simplified model © 2017 American Chemical Society
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DOI: 10.1021/acs.chemrev.9b00105 Chem. Rev. XXXX, XXX, XXX−XXX
