| Description | The oxidative decarboxylation of pyruvate to acetyl-CoA, a central step in energy metabolism, can occur by two different mechanisms [ ]. In mitochondria and aerobic bacteria this reaction is catalysed by the multienzyme complex pyruvate dehydrogenase using NAD as electron acceptor. In anaerobic organisms, however, this reaction is reversibly catalysed by a single enzyme using either ferrodoxin or flavodoxin as the electron acceptor.Pyruvate:ferrodoxin/flavodoxin reductases (PFORs) in this entry occur in both obligately and facultatively anaerobic bacteria and also some eukaryotic microorganisms. These proteins are single-chain enzymes containing a thiamin pyrophosphate cofactor for the cleavage of carbon-carbon bonds next to a carbonyl group, and iron-sulphur clusters for electron transfer. The Desulfovibrio africanus enzyme is currently the only PFOR whose three dimensional structure is known [ , ]. It is a homodimer where each subunit contains one thiamin pyrophosphate cofactor and two ferrodoxin-like 4Fe-S clusters and an atypical 4Fe-S cluster. Each monomer is composed of seven domains - domains I, II and VI make intersubunit contacts, while domains III, IV and V are located at the surface of the dimer, and domain VII forms a long arm extending over the other subunit. The cofactor is bound at the interface of domains I and VI and is proximal to the atypical 4Fe-S bound by domain VI, while the ferrodoxin-like 4Fe-S clusters are bound by domain V. Comparison of this enzyme with the multi-chain PFORs shows a correspondence between the domains in this enzyme and the subunits of the multi-chain enzymes. | Name | Pyruvate-flavodoxin oxidoreductase |
| Short Name | Pyrv_flavodox_OxRed | Type | Family |
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