Properties of Nicotinamide Adenine Dinucleotide Phosphate-Dependent Formate Dehydrogenase from Clostridium thermoaceticum

Lan-Fun Li, Lars Ljungdahl, Harland G. Wood
1966 Journal of Bacteriology  
Li, LAN-FUN (Western Reserve University School of Medicine, Cleveland, Ohio), LARs LJUNGDAHL, AND HARLAND G. WooD. Properties of nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from Clostridium thermoaceticum. J. Bacteriol. 92: 405-412. 1966.-A nicotinamide adenine dinucleotide phosphate (NADP)-dependent formate dehydrogenase has been isolated from C. thermoaceticum. The enzyme is very sensitive to oxygen and requires sulfhydryl compounds for activity. The apparent
more » ... ity. The apparent Km at 50 C and pH 7.0 for NADP is 5.9 x 10-M and for formate, 2.2 X 10-4 M. The enzyme is most active at about 60 C and at pH values between 7.0 and 9.0. The enzyme catalyzes an exchange between Ci402 and formate, which requires NADP, but net synthesis of formate from CO2 and reduced nicotinamide adenine dinucleotide phosphate could not be demonstrated. The reaction does not involve ferredoxin. assay mixture contained (,moles/ml): potassium phosphate buffer (pH 7.0), 100; NADP, 1; cysteine, 40; formate, 20; and B12 (cyanocobalamin), 0.35. 405 on May 9, 2020 by guest
doi:10.1128/jb.92.2.405-412.1966 fatcat:hmj74kvwgfcu7kxcu743mxgl3u