KINETICS AND MECHANISMS OF ELECTRON-TRANSFER BETWEEN BLUE COPPER PROTEINS AND ELECTRONICALLY EXCITED CHROMIUM AND RUTHENIUM POLYPYRIDINE COMPLEXES
KINETICS AND MECHANISMS OF ELECTRON-TRANSFER BETWEEN BLUE COPPER PROTEINS AND ELECTRONICALLY EXCITED CHROMIUM AND RUTHENIUM POLYPYRIDINE COMPLEXES
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DOI：
10.1021/ic00217a010
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发表时间：
1985-01-01
影响因子：
4.6
通讯作者：
GRAY, HB
中科院分区：
文献类型：
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作者：
BRUNSCHWIG, BS;DELAIVE, PJ;GRAY, HB
在水溶液中研究了铜蛋白质体青苷、蓝蛋白和星青苷对CrL33+和RuL32+络合物（L为1,10 -菲罗啉和2,2 '-联吡啶或取代衍生物）的猝灭动力学。Cu (I)蛋白的猝灭速率常数在高蛋白浓度下接近~ 106 s-1的极限值。根据金属配合物在距离铜中心10- 12a远的位点结合的模型，讨论了质体青素的动力学行为。该模型允许电子从这个遥远的位置转移，也允许通过靠近铜中心的金属配合物的攻击转移。结果表明，在低蛋白浓度下，邻近途径比远端途径快10倍左右。分子内电子从远处转移的速率常数与理论计算的期望值一致。
The kinetics of the quenching of the long-livedexcited states of CrL33+ and RuL32+ complexes (L is 1, 10-phenanthroline and2, 2'-bipyridine or substituted derivatives) by the copper proteins plastocyanin, azurin, and stellacyanin have been studied in aqueous solution. The rate constants for quenching by the Cu (I) proteins approach a limiting value of~ 106 s-1 at high protein concentration. The kinetic behavior for plastocyanin is discussed in terms of a model in which the metal complex binds at a remote site 10-12 A from the coppercenter. The model allows for electron transfer both from this remote site and by attack of the metal complex adjacent to the copper center. The results show that at low protein concentration the adjacent pathway is about 10 times faster than theremote pathway. The rate constant for the intramolecular electron transfer from theremote site is consistent with the value expected on the basis of theoretical calculations.