The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Proton-Coupled Electron Flow in Protein Redox Machines
Open accessAbstract
Electron transfer (ET) reactions are fundamental steps in biological redox processes. Respiration is a case in point: at least 15 ET reactions are required to take reducing equivalents from NADH, deposit them in O_2, and generate the electrochemical proton gradient that drives ATP synthesis. Most of these reactions involve quantum tunneling between weakly coupled redox cofactors (ET distances > 10 Å) embedded in the interiors of folded proteins. Here we review experimental findings that have shed light on the factors controlling these distant ET events. We also review work on a sensitizer-modified copper protein photosystem in which multistep electron tunneling (hopping) through an intervening tryptophan is orders of magnitude faster than the corresponding single-step ET reaction.If proton transfers are coupled to ET events, we refer to the processes as proton coupled ET, or PCET, a term introduced by Huynh and Meyer in 1981. Here we focus on two protein redox machines, photosystem II and ribonucleotide reductase, where PCET processes involving tyrosines are believed to be critical for function. Relevant tyrosine model systems also will be discussed.
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Cites
Proton-coupled electron transfer
Huynh, M. H. V., & Meyer, T. J. (2007) · Chemical Reviews · doi:10.1021/cr0500030 · Cited by 1,659
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253
Stubbe, J., Nocera, D. G., Yee, C. S., & Chang, M. C. Y. (2003) · Chemical Reviews · doi:10.1021/cr020421u · Cited by 823
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
Sazanov, L. A., & Hinchliffe, P. (2006) · Science · doi:10.1126/science.1123809 · Cited by 763
Reece, S. Y., Hodgkiss, J. M., Stubbe, J., & Nocera, D. G. (2006) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2006.1874 · Cited by 294
Chang, C. J., Chang, M. C. Y., Damrauer, N. H., & Nocera, D. G. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2003.08.010 · Cited by 189
Metadata
- Authors
- Dempsey, J. L., Winkler, J. R., & Gray, H. B.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-11-17
- Volume
- 110
- Issue
- 12
- Pages
- 7024-7039
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1986670180
- Cited by
- 299
- References
- 6
- FWCI
- 0.67
- Type
- journal article
- Language
- en
- Open access
- green
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