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

FEBS Letters

Guerlesquin, Françoise²  Hatchikian, Claude²  ElAntak, Latifa²  Morelli, Xavier²  Czjzek, Mirjam¹  Dolla, Alain²  Bornet, Olivier² 

[1] Unité de Architecture et Fonction des Macromolécules Biologiques, IBSM-CNRS, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France;Unité de Bioénergétique et Ingénierie des Protéines, IBSM-CNRS, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France

关键词: Electron transfer;    Cytochrome;    [Fe]-hydrogenase;    NMR;    Docking;   

DOI  :  10.1016/S0014-5793(03)00718-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cytochrome c₃ (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 c₃–[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 c₃ is an electron shuttle between the periplasmic hydrogenase and the Hmc membrane-bound complex.

【 授权许可】

Unknown