Modelling the electron-transfer complex between aldehyde oxidoreductase and flavodoxin

Ludwig Krippahl; P. Nuno Palma; Isabel Moura; José J. G. Moura

doi:10.1002/ejic.200600418

Modelling the electron-transfer complex between aldehyde oxidoreductase and flavodoxin

Ludwig Krippahl, P. Nuno Palma, Isabel Moura, José J. G. Moura

Research output: Contribution to journal › Article

8 Citations (Scopus)

Abstract

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 electrontransfer pathway are observed.

Original language	English
Pages (from-to)	3835-3840
Number of pages	6
Journal	European Journal of Inorganic Chemistry
Issue number	19
DOIs	https://doi.org/10.1002/ejic.200600418
Publication status	Published - 2 Oct 2006

Keywords

Bioinorganic chemistry
Electron transfer
Enzyme models
Molybdenum

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10.1002/ejic.200600418Licence: CC BY-NC

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Krippahl, L., Palma, P. N., Moura, I., & Moura, J. J. G. (2006). Modelling the electron-transfer complex between aldehyde oxidoreductase and flavodoxin. European Journal of Inorganic Chemistry, (19), 3835-3840. https://doi.org/10.1002/ejic.200600418

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AB - 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 electrontransfer pathway are observed.

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