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The cytochrome c3-[Fe]-hydrogenase electron-transfer complex: structural model by NMR restrained docking
Latifa ElAntak1, Xavier Morelli, Olivier Bornet
1Unité de Bioénergétique et Ingénierie des Protéines, IBSM-CNRS, 31 chemin Joseph Aiguier, 13402 Cedex 20, Marseille, France. guerlesq@ibsm.cnrs-mrs.fr
FEBS Letters
|July 30, 2003
Summary
Cytochrome c(3) acts as an electron shuttle in sulfate-reducing bacteria. A structural model reveals its connection to [Fe]-hydrogenase, facilitating electron transfer to the Hmc complex.
Area of Science:
- Biochemistry
- Microbiology
- Structural Biology
Background:
- Cytochrome c(3) is a low redox potential tetrahemic protein crucial for anaerobic metabolism in sulfate-reducing bacteria.
- It functions as an electron transfer intermediate between [Fe]-hydrogenase and the Hmc complex in Desulfovibrio vulgaris.
Purpose of the Study:
- To elucidate the structural interactions within the cytochrome c(3)-[Fe]-hydrogenase complex.
- To understand the role of cytochrome c(3) as an electron shuttle in Desulfovibrio vulgaris.
Main Methods:
- Nuclear magnetic resonance (NMR) restrained docking was employed to generate a structural model.
- The model visualizes the complex formed between cytochrome c(3) and [Fe]-hydrogenase.
Main Results:
- A structural model of the cytochrome c(3)-[Fe]-hydrogenase complex was successfully obtained.
- The model shows a direct connection between the distal cluster of [Fe]-hydrogenase and heme 4 of cytochrome c(3).
- This heme (heme 4) is also involved in the interaction with cytochrome Hmc.
Conclusions:
- Cytochrome c(3) serves as a vital electron shuttle, connecting the periplasmic [Fe]-hydrogenase to the membrane-bound Hmc complex.
- The structural model provides key insights into the electron transfer pathway in sulfate-reducing bacteria.