InterPro domain: IPR036683

Proteins containing this domain form structural complexes with other known families, such as IPR008274 and IPR001041 . The carbon monoxide (CO) dehydrogenase of Oligotropha carboxidovorans is a heterotrimeric complex composed of a apoflavoprotein, a molybdoprotein, and an iron-sulphur protein. It can be dissociated with sodium dodecylsulphate [ 1 ]. CO dehydrogenase catalyzes the oxidation of CO according to the following equation [ 2 ]: CO + H2O = CO2 + 2e + 2H+

Subunit S represents the iron-sulphur protein of CO dehydrogenase and is clearly divided into a C- and an N-terminal domain, each binding a [2Fe-2S] cluster [ 3 ].

The structure of the C-terminal domain has a beta(3,4)-alpha(3) fold arranged in an alpha+beta sandwich.

1. Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli. J. Biol. Chem. 275, 1864-72
2. The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase. Biol. Chem. 381, 865-76
3. Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. Proc. Natl. Acad. Sci. U.S.A. 96, 8884-9