Modelling the electron-transfer complex between aldehyde oxidoreductase and flavodoxin

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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 languageEnglish
Pages (from-to)3835-3840
Number of pages6
JournalEuropean Journal of Inorganic Chemistry
Issue number19
Publication statusPublished - 2 Oct 2006


  • Bioinorganic chemistry
  • Electron transfer
  • Enzyme models
  • Molybdenum


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