期刊
CHEMICAL REVIEWS
卷 121, 期 4, 页码 2020-2108出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.chemrev.0c00712
关键词
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资金
- National Science Centre, Poland [2015/18/A/NZ1/00046]
- Foundation for Polish Science [POIR.04.04.00-00-5B54/17-00]
- U.S. National Institutes of Health/General Medical Sciences [GMS-038323]
- U.S. Dept. of Energy [DOE DE-SC0018238]
- French national funding agency ANR [ANR-17-CE05-0029]
- excellence cluster LabEX GRAL within the University Grenoble Alpes graduate school -Ecoles Universitaires de Recherche-CBHEUR-GS [ANR-10LABX-49-01, ANR-17-EURE-0003]
- European Research Council (ERC AdG Chloro-mito) [833184]
- Priority Research Area BioS under the program Excellence Initiative Research University at the Jagiellonian University
- U.S. Department of Energy (DOE) [DE-SC0018238] Funding Source: U.S. Department of Energy (DOE)
- European Research Council (ERC) [833184] Funding Source: European Research Council (ERC)
This review focuses on the key components of respiratory and photosynthetic energy-transduction systems - the Cytbc(1)/b(6)f complexes. While these enzymes have been extensively studied, there are still important aspects of their molecular mechanisms that require further elucidation.
This review focuses on key components of respiratory and photosynthetic energy-transduction systems: the cytochrome bc(1) and b(6)f (Cytbc(1)/b(6)f) membranous multisubunit homodimeric complexes. These remarkable molecular machines catalyze electron transfer from membranous quinones to water-soluble electron carriers (such as cytochromes c or plastocyanin), coupling electron flow to proton translocation across the energy-transducing membrane and contributing to the generation of a transmembrane electrochemical potential gradient, which powers cellular metabolism in the majority of living organisms. Cytsbc(1)/b(6)f share many similarities but also have significant differences. While decades of research have provided extensive knowledge on these enzymes, several important aspects of their molecular mechanisms remain to be elucidated. We summarize a broad range of structural, mechanistic, and physiological aspects required for function of Cytbc(1)/b(6)f, combining textbook fundamentals with new intriguing concepts that have emerged from more recent studies. The discussion covers but is not limited to (i) mechanisms of energy-conserving bifurcation of electron pathway and energy-wasting superoxide generation at the quinol oxidation site, (ii) the mechanism by which semiquinone is stabilized at the quinone reduction site, (iii) interactions with substrates and specific inhibitors, (iv) intermonomer electron transfer and the role of a dimeric complex, and (v) higher levels of organization and regulation that involve Cytsbc(1)/b(6)f. In addressing these topics, we point out existing uncertainties and controversies, which, as suggested, will drive further research in this field.
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