Contains [4Fe-4S] and a mononucleotide molybdenum (pyranopterin) cofactor. Has broad substrate specificity, with 2-oxo-monocarboxylates and 2-oxo-dicarboxylates acting as substrates. Branching in a substrate at the C-3 position results in loss of activity. The enzyme from Proteus sp. is inactivated by oxygen.
Trautwein, T., Krauss, F., Lottspeich, F. and Simon, H. The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. Eur. J. Biochem.222 (1994) 1025–1032. [DOI] [PMID: 8026480]
Neumann, S. and Simon, H. On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species. FEBS Lett.167 (1985) 29–32.