期刊
COORDINATION CHEMISTRY REVIEWS
卷 256, 期 21-22, 页码 2478-2487出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ccr.2012.03.032
关键词
Electron transfer; Multistep tunneling; Hopping maps; Redox proteins azurin; Ribonucleotide reductase; DNA photolyase; MauG
资金
- NIH, an NSF Center for Chemical Innovation (Powering the Planet) [DK019038, GM095037, CHE-0947829]
- Czech Ministry of Education [ME 10124]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0802907] Funding Source: National Science Foundation
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 angstrom 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. (C) 2012 Elsevier B.V. All rights reserved.
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