ELECTRON PROTON COUPLING IN CYTOCHROME-C STUDIED USING PROTEIN VARIANTS

被引:26
作者
GAO, Y
MCLENDON, G
PIELAK, GJ
WILLIAMS, RJP
机构
[1] UNIV OXFORD,INORGAN CHEM LAB,S PARKS RD,OXFORD OX1 3QR,ENGLAND
[2] UNIV ROCHESTER,DEPT CHEM,ROCHESTER,NY 14627
[3] UNIV N CAROLINA,DEPT BIOCHEM,CHAPEL HILL,NC 27514
[4] UNIV N CAROLINA,PROGRAM MOLEC BIOL & BIOTECHNOL,CHAPEL HILL,NC 27514
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 204卷 / 01期
关键词
D O I
10.1111/j.1432-1033.1992.tb16642.x
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
An NMR study of the cytochrome c variant Asn52Ile is used to show how the redox state change in native cytochrome c is coupled to a rearrangement of a proton network which runs through the cytochrome c molecule. The substitution breaks the H-bond network and removes the coupling. The uncovering of this putative proton channel and the connection of changes to it with redox state changes of the iron centre of the protein allows a possible description of the way in which redox energy state changes can be coupled to energisation and gating of protons in membranes.
引用
收藏
页码:337 / 352
页数:16
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