Modelling the Electron-Transfer Complex Between Aldehyde Oxidoreductase and Flavodoxin

Three‐dimensional protein structures of the xanthine oxidase family show different solutions for the problem of transferring electrons between the flavin adenine dinucleotide (FAD) group and the molybdenum cofactor. In xanthine oxidase all the cofactors lie within domains of the same protein chain,...

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Bibliographic Details
Published in:European Journal of Inorganic Chemistry 2006-10, Vol.2006 (19), p.3835-3840
Main Authors: Krippahl, Ludwig, Palma, P. Nuno, Moura, Isabel, Moura, José J. G.
Format: Article
Language:English
Subjects:
Bioinorganic chemistry
Electron transfer
Enzyme models
Molybdenum
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Summary:Three‐dimensional protein structures of the xanthine oxidase family show different solutions for the problem of transferring electrons between the flavin adenine dinucleotide (FAD) group and the molybdenum cofactor. In xanthine oxidase all the cofactors lie within domains of the same protein chain, whereas in CO dehydrogenase the Fe–S centres, FAD and Mo cofactors are enclosed in separate chains and the enzyme exists as a stable complex of all three. In aldehyde oxidoreductase, only Fe–S and Mo co‐factors are present in a single protein chain. Flavodoxin is docked to aldehyde oxidoreductase to mimic the flavin component on the intramolecular electron transfer chain of aanthine oxidase and CO dehydrogenase and, remarkably, the main features of the electron‐transfer pathway are observed. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006)
ISSN:1434-1948
1099-0682
DOI:10.1002/ejic.200600418