Electron-transfer mechanisms through biological redox chains in multicenter enzymes.

Journal article

A new approach for studying intramolecular electron transfer in multicenter enzymes is described. Two fumarate reductases, adsorbed on an electrode in a fully active state, have been studied using square-wave voltammetry as a kinetic method to probe the mechanism of the long-range electron transfer to and from the buried active site. Flavocytochrome c(3) (Fcc(3)), the globular fumarate reductase from Shewanella frigidimarina, and the soluble subcomplex of the membrane-bound fumarate reductase...

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Authors: Jeuken, L; Jones, A; Chapman, S; Cecchini, G; Armstrong, F

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 124
• Issue: 20
• Pages: 5702-5713
• Publication date: 2002-05-01
• DOI: 10.1021/ja012638w
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Escherichia coli; Models, Chemical; Kinetics; Flavin-Adenine Dinucleotide; Cytochrome c Group; Oxidation-Reduction; Binding Sites; Protein Conformation; Succinate Dehydrogenase; Electrons; Benzoquinones; Computer Simulation; Shewanella; Heme