The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Electron hopping through proteins
Open accessAbstract
Biological redox machines require efficient transfer of electrons and holes for function. Reactions involving multiple tunneling steps, termed “hopping,” often promote charge separation within and between proteins that is essential for energy storage and conversion. Here we show how semiclassical electron transfer theory can be extended to include hopping reactions: graphical representations (called hopping maps) of the dependence of calculated two-step reaction rate constants on driving force are employed to account for flow in a rhenium-labeled azurin mutant as well as in two structurally characterized redox enzymes, DNA photolyase and MauG. Analysis of the 35 Å radical propagation in ribonucleotide reductases using hopping maps shows that all tyrosines and tryptophans on the radical pathway likely are involved in function. We suggest that hopping maps can facilitate the design and construction of artificial photosynthetic systems for the production of fuels and other chemicals.
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Cites
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
Direct observation of thymine dimer repair in DNA by photolyase
Kao, Y.-T., Saxena, C., Wang, L., Sancar, A., & Zhong, D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506586102 · Cited by 259
Cited by
Oxidative cleavage of polysaccharides by monocopper enzymes depends on H2O2
Bissaro, B., Røhr, Å. K., Müller, G., Chylenski, P., Skaugen, M., Forsberg, Z., Horn, S. J., Vaaje-Kolstad, G., & Eijsink, V. G. H. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2470 · Cited by 594
Biochemistry and Theory of Proton-Coupled Electron Transfer
Migliore, A., Polizzi, N. F., Therien, M. J., & Beratan, D. N. (2014) · Chemical Reviews · doi:10.1021/cr4006654 · Cited by 520
Recent Advances in the Theory and Molecular Simulation of Biological Electron Transfer Reactions
Blumberger, J. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00298 · Cited by 450
Photoexcitation of flavoenzymes enables a stereoselective radical cyclization
Biegasiewicz, K. F., Cooper, S. J., Gao, X., Oblinsky, D. G., Kim, J. H., Garfinkle, S. E., Joyce, L. A., Sandoval, B. A., Scholes, G. D., & Hyster, T. K. (2019) · Science · doi:10.1126/science.aaw1143 · Cited by 445
Winkler, J. R., & Gray, H. B. (2014) · Journal of the American Chemical Society · doi:10.1021/ja500215j · Cited by 306
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Metadata
- Authors
- Warren, J. J., Ener, M. E., Vlček, A., Winkler, J. R., & Gray, H. B.
- Venue
- Coordination Chemistry Reviews
- Publisher
- Elsevier BV
- Published
- 2012-11
- Volume
- 256
- Issue
- 21-22
- Pages
- 2478-2487
- ISSN
- 0010-8545 (ISSN-L)
- OpenAlex
- W2045446729
- Cited by
- 169
- References
- 4
- FWCI
- 5.22
- Type
- journal article
- Language
- en
- Open access
- bronze
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