Electron Transfer Mechanisms in Heme Proteins
作者:
MichaelA. Cusanovich,
JamesT. Hazzard,
TerranceE. Meyer,
Gordon Tollin,
期刊:
Journal of Macromolecular Science: Part A - Chemistry
(Taylor Available online 1989)
卷期:
Volume 26,
issue 2-3
页码: 433-443
ISSN:0022-233X
年代: 1989
DOI:10.1080/00222338908051985
出版商: Taylor & Francis Group
数据来源: Taylor
摘要:
Recent years have seen substantial progress in our understanding of biological electron-transfer mechanisms. Of particular value have been soluble c-type cytochromes, due to the large structural base available. Using structurally homologous families of simple redox proteins, the contribution of driving force, electrostatics, and sterics to the kinetics of electron transfer has been quantified. Importantly, because Marcus' theory for outer-sphere electron transfer is applicable, we have been able to develop an approach termed “kinetic taxonomy.” That is, based on the correlations obtained with a large number of redox proteins in different structural families, we can predict structural features from the kinetic properties of redox proteins of unknown structure. More recently, we have been able to establish a role for dynamics, orientation, and intervening media in intracomplex electron transfer when two redox proteins form a long-lived complex.
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