期刊
QUARTERLY REVIEWS OF BIOPHYSICS
卷 48, 期 4, 页码 411-420出版社
CAMBRIDGE UNIV PRESS
DOI: 10.1017/S0033583515000062
关键词
electron transfer; protein radical; hole hopping; azurin; cytochrome P450
类别
资金
- National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health [R01DK019038]
- Arnold and Mabel Beckman Foundation
Biological electron transfers often occur between metal-containing cofactors that are separated by very large molecular distances. Employing photosensitizer-modified iron and copper proteins, we have shown that single-step electron tunneling can occur on nanosecond to microsecond timescales at distances between 15 and 20 angstrom. We also have shown that charge transport can occur over even longer distances by hole hopping (multistep tunneling) through intervening tyrosines and tryptophans. In this perspective, we advance the hypothesis that such hole hopping through Tyr/Trp chains could protect oxygenase, dioxygenase, and peroxidase enzymes from oxidative damage. In support of this view, by examining the structures of P450 (CYP102A) and 2OG-Fe (TauD) enzymes, we have identified candidate Tyr/Trp chains that could transfer holes from uncoupled high-potential intermediates to reductants in contact with protein surface sites.
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