Formate dehydrogenase, Clostridium

Yamamoto I, T Saiki, S-M Liu, LG Ljungdahl (1983) Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein. J Biol Chem 258 1826-1832. 

Andreesen JR, Ljungdahl LG. 1973. Formate dehydrogenase of Clostridium ther-moaceticum incorporation of selenium-75, and the effects of selenite, molybdate, and tnngstate on the enzyme. J Bacteriol 116 867-73. 

Clostridium peifringens ferredoxin, 38 261 Clostridium thermoaceticum, 32 326 carboxylic acid reductase, 40 73 CO dehydrogenase, 38 362 formate dehydrogenase, 40 71-72 CISCN, 33 81... 

Nicotinic acid hydroxylase from Clostridium barkerii catalyzes reaction (55), the hydroxylation of a pyridine group, and has similarities to xanthine dehydrogenase. Nicotinic acid hydroxylase is a 300 000 molecular weight flavoprotein containing iron-sulfur and FAD centres, selenium1034 and a molybdopterin cofactor.1035 Formate dehydrogenase contains selenium as selenocysteine,1036 but this does not appear to be the case for nicotinic acid hydroxylase. The possibility that the selenium is incorporated into the molybdopterin cannot be excluded at present. 

Acetogenesis and the primary structure of the NADP-dependent formate dehydrogenase of Clostridium thermoaceticum, a tungsten-selenium-iron protein. 

Ljungdahl LG and Andeeseen JR (1975) Tungsten, a component of active formate dehydrogenase from Clostridium thermoacetium. FEES Lett 64 279-282. 

Acetogenic bacteria such as Clostridium (Cl.) ther-moaceticum or Cl. formicoaceticum catalyze an NADPH2-driven CO2 reduction to formate, which is further reduced via the tetrahydrofolate pathway to the -CH3 oxidation state, as the methyl is finally incorporated into acetic acid. This anabolic formate dehydrogenase has long been known to depend on the presence of Se in the medium for its formation. The enzyme is an ai 2 heterooligomer of 340 kDa the complex contains two selenocysteine residues, two moles of a tungsten cofactor, and Fe/S centers. 

Residues of the selenoamino acid, selenocysteine, are present in bacterial formate dehydrogenase (E.coli), and glycine reductase (Clostridium). [T.C Stadtman Advances in Enzymology 48 (1979) 1-28]... 

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