Characterization and spectroscopic properties of reduced Mo and W formate dehydrogenase from C. thermoaceticum.
Formate dehydrogenase (FDH) (EC 1.2.1.43) from C. thermoaceticum has been purified in two forms. One contains tungsten (W), and the other is enriched in molybdenum (Mo). The W-FDH is clearly active, while the Mo results are ambiguous with enzymatic activities generally lower in the Mo-enriched samples. Spectroscopic studies (EPR, absorption, and CD) on W-FDH and Mo-FDH demonstrate that no signal correlates to the group VI metal active site in the dithionite-reduced enzyme. This lack of a W(V) EPR signal is in contrast to the results observed for tungsten-substituted sulfite oxidase which is inactive.
D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D001665:Binding Sites; D002942:Circular Dichroism; D003013:Clostridium / Q000201:enzymology*; D004578:Electron Spin Resonance Spectroscopy; D004789:Enzyme Activation; D005560:Formate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D008982:Molybdenum / Q000032:analysis; D011487:Protein Conformation; D013053:Spectrophotometry; D014414:Tungsten / Q000032:analysis
D008982:Molybdenum; D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases; D014414:Tungsten