| Description | Carbon monoxide dehydrogenases catalyse the reversible oxidation of carbon monoxide to carbon dioxide as shown below [ , ]:CO + H(2)O + A == CO(2) + AH(2)A variety of electron acceptors can be used by these enzymes including ferredoxin, methyl viologen and benzyl viologen. Under anaerobic conditions, carbon monoxide is utilised by a number of methanogenic archaea and acetogenic, sulphate-reducing or phototrophic bacteria. Under aerobic conditions carbon monoxide can be used as sole carbon and energy source by the carboxidotrophic bacteria, a taxonomically diverse group of obligate or facultative chemolithoautotrophic species. The anaerobic dehydrogenases are mostly nickel-containing iron-sulphur enzymes, while the The aerobic enzymes categorised so far are molybdenum-containing iron-sulphur proteins.This entry represents the large subunit of the molybdenum-containing carbon monoxide dehydrogenase found in aerobic bacteria. This enzyme is a dimer of heterotrimers, where each heterotrimer consists of a small iron-sulphur subunit, a medium FAD-containing flavoprotein subunit and a large molybdopterin-containign subunit which contains the active site [ , ]. The large subunit is divided into two domains. The N-terminal domain is composed of mainly of a five-and four-stranded mixed β-sheet and interacts with the small and medium subunits. The C-terminal domain contains a region which interacts with its counterpart in the overall dimer, providing the main dimer contact, and a β-sheet surrounded by α helices. The active site located in this subunit contains a novel dinuclear heterometal [CuSMo(=O)OH]cluster. | Name | Carbon-monoxide dehydrogenase, large subunit |
| Short Name | CO_Mo_DH_lsu | Type | Family |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
