共 51 条
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
相关论文