Abstract
AbstractThree‐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)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callSimilar Papers
More From: European Journal of Inorganic Chemistry
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
