Differential influence of dynamic processes on forward and reverse electron transfer across a protein-protein interface

被引：58

作者：

Hoffman, BM ^{[1
]}

Celis, LM ^{[1
]}

Cull, DA ^{[1
]}

Patel, AD ^{[1
]}

Seifert, JL ^{[1
]}

Wheeler, KE ^{[1
]}

Wang, JY ^{[1
]}

Yao, J ^{[1
]}

Kurnikov, IV ^{[1
]}

Nocek, JM ^{[1
]}

机构：

[1] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2005年 / 102卷 / 10期

关键词：

cytochrome c; dynamics; hemoglobin; myoglobin; cytochrome c peroxidase;

D O I：

10.1073/pnas.0408767102

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We propose that the forward and reverse halves of a flash-induced protein-protein electron transfer (ET) photocycle should exhibit differential responses to dynamic interconversion of configurations when the most stable configuration is not the most reactive, because the reactants exist in different initial configurations: the flash-photoinitiated forward ET process begins with the protein partners in an equilibrium ensemble of configurations, many of which have little or no reactivity, whereas the reactant of the thermal back ET (the charge-separated intermediate) is formed in a nonequillbrium, "activated" protein configuration. We report evidence for this proposal in measurements on (i) mixed-metal hemoglobin hybrids, (it) the complex between cytochrome c peroxidase and cytochrome c, and (iii and iv) the complexes of myoglobin and isolated hemoglobin alpha-chains with cytochrome b(5). For all three systems, forward and reverse ET does respond differently to modulation of dynamic processes; further, the response to changes in viscosity is different for each system.

引用

页码：3564 / 3569

页数：6

共 51 条

[1]

[Anonymous], 1989, Chemical Kinetics and Dynamics

[2]

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