The cytochrome c3-[Fe]-hydrogenase electron-transfer complex:: structural model by NMR restrained docking

被引:33
作者
ElAntak, L
Morelli, X
Bornet, O
Hatchikian, C
Czjzek, M
Alain, DA
Guerlesquin, F
机构
[1] CNRS, IBSM, Unite Bioenerget & Ingn Prot, F-13402 Marseille 20, France
[2] CNRS, IBSM, Unite Architecture & Fonct Macromol Biol, F-13402 Marseille, France
关键词
electron transfer; cytochrome; Fe]-hydrogenase; NMR; docking;
D O I
10.1016/S0014-5793(03)00718-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
Cytochrome c(3) (M-r 13 000) is a low redox potential cytochrome specific of the anaerobic metabolism in sulfate-reducing bacteria. This tetrahemic cytochrome is an intermediate between the [Fe]-hydrogenase and the cytochrome Hmc in Desulfovibrio vulgaris Hildenborough strain. The present work describes the structural model of the cytochrome c(3)-[Fe]-hydrogenase complex obtained by nuclear magnetic resonance restrained docking. This model connects the distal cluster of the [Fe]-hydrogenase to heme 4 of the cytochrome, the same heme found in the interaction with cytochrome Hmc. This result gives evidence that cytochrome c(3) is an electron shuttle between the periplasmic hydrogenase and the Hmc membrane-bound complex. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:1 / 4
页数:4
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