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Published December 15, 2011 | public
Book Section - Chapter

Aldehyde Ferredoxin Oxidoreductase


Aldehyde ferredoxin oxidoreductase (AOR) is a homodimer where each subunit contains a [4Fe–4S] cluster and a mononuclear tungsten atom coordinated by the dithioline groups of two pterin molecules. The two subunits of the dimer are bridged by a monomeric iron site. AOR is a member of a family of five closely related tungstoenzymes found in organisms that grow at high temperatures in marine volcanic vents. The enzyme catalyzes the two-electron oxidation of its aldehyde substrate to the corresponding acid with the concomitant reduction of ferredoxin, its physiological electron acceptor. The enzyme can oxidize a wide range of aliphatic and aromatic aldehydes. The most efficient substrates for AOR are acetaldehyde, isovaleraldehyde, phenylacetaldehyde, and indoleacetaldehyde, the aldehyde derivatives of some of the most common amino acids.

Additional Information

© 2011 John Wiley & Sons, Ltd. Published Online: 15 DEC 2011. Research on tungstoenzymes carried out in the authors' laboratories was supported by grants from the Department of Energy, the National Science Foundation and the National Institutes of Health.

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