Electron tunneling in proteins: Role of the intervening medium

被引:94
作者
Winkler, JR
Gray, HB
机构
[1] Beckman Institute, California Institute of Technology, Pasadena
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 1997年 / 2卷 / 03期
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
RUTHENIUM-MODIFIED PROTEINS; BLUE COPPER PROTEINS; PATHWAY ANALYSIS; CYTOCHROME-C; DISTANCE; RATES; ABINITIO; OXIDASE; MODEL; SITE;
D O I
10.1007/s007750050150
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Analysis of electron-transfer (ET) kinetics data obtained from experiments on Ru-modified proteins (cytochrome c, azurin, myoglobin) reveals that distant donor-acceptor electronic couplings depend upon the secondary structure of the intervening polypeptide matrix. Rates of Fe2+ --> RU3+ ET reactions in cytochrome c decay exponentially with tunneling-pathway length (decay constant 0.73 Angstrom(-1)); these rates also decay exponentially with Ru-Fe distance (decay constant In azurin, a beta-sheet protein, Cu+ --> Ru3+ rates exhibit an exponential Cu-Ru distance dependence with a decay constant of 1.1 Angstrom(-1) Comparison of distant couplings in azurin and myoglobin suggests that hydrogen bonds are better mediators across beta sheets than through alpha helices.
引用
收藏
页码:399 / 404
页数:6
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