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- W1566131755 abstract "Formate dehydrogenase from Clostridiun pasteurianum catalyses the interconversion of CO 2 , and formate. It is a complex enzyme, containing molybdenum, iron, acid‐labile sulfur and pterin. Redox potentiometry and EPR analysis reveal two spectrally and thermodynamically distinct iron‐sulfur clusters, with g 1.87, 1.95 and 2.05 ( E m8 ‐318 mV) and g 1.92 and 2.05 ( E m8 ‐372 mV), both present at approx. 0.3 spins per enzyme. There is also a free radical signal centered near g 2.005 which we attribute to the pterin, perhaps in its anionic semiquinone form. This signal disappears on oxidation ( E m8 ‐150 mV), but is not reduced further at pH 8. It is present at approx. 0.8 spins per enzyme. No EPR signals attributable to the molybdenum were detected." @default.
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- W1566131755 date "1985-09-23" @default.
- W1566131755 modified "2023-10-14" @default.
- W1566131755 title "Formate dehydrogenase from<i>Clostridium pasteurianum</i>" @default.
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- W1566131755 doi "https://doi.org/10.1016/0014-5793(85)81036-x" @default.
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