The cytochrome c3-[Fe]-hydrogenase electron-transfer complex: structural model by NMR restrained docking
| Autor: | Mirjam Czjzek, Latifa Elantak, Françoise Guerlesquin, Alain Dolla, Claude E. Hatchikian, Xavier Morelli, Olivier Bornet |
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| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Cytochrome Stereochemistry Biophysics Cytochrome c Group Biochemistry [Fe]-hydrogenase Docking Electron transfer Electron Transport Cytochrome C1 Structural Biology Genetics Cytochrome c oxidase Desulfovibrio vulgaris Nuclear Magnetic Resonance Biomolecular Molecular Biology biology Cytochrome b Chemistry Cytochrome b6f complex Cytochrome c peroxidase Cytochrome c Membrane Proteins Cell Biology NMR Coenzyme Q – cytochrome c reductase biology.protein Periplasmic Proteins Oxidoreductases Oxidation-Reduction Protein Binding |
| Zdroj: | FEBS Letters. 548:1-4 |
| ISSN: | 0014-5793 |
| Popis: | Cytochrome c3 (Mr 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. |
| Databáze: | OpenAIRE |
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