Li L F, Ljungdahl L, Wood H G
Department of Biochemistry, Western Reserve University, School of Medicine, Cleveland, Ohio.
J Bacteriol. 1966 Aug;92(2):405-12. doi: 10.1128/jb.92.2.405-412.1966.
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 K(m) at 50 C and pH 7.0 for NADP is 5.9 x 10(-5)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 C(14)O(2) and formate, which requires NADP, but net synthesis of formate from CO(2) and reduced nicotinamide adenine dinucleotide phosphate could not be demonstrated. The reaction does not involve ferredoxin.
李兰芬（俄亥俄州克利夫兰市西储大学医学院）、拉尔斯·永达尔和哈兰德·G·伍德。嗜热醋酸梭菌中烟酰胺腺嘌呤二核苷酸磷酸依赖性甲酸脱氢酶的性质。《细菌学杂志》92: 405 - 412。1966年。——已从嗜热醋酸梭菌中分离出一种烟酰胺腺嘌呤二核苷酸磷酸（NADP）依赖性甲酸脱氢酶。该酶对氧气非常敏感，其活性需要巯基化合物。在50℃和pH 7.0条件下，该酶对NADP的表观米氏常数（K(m)）为5.9×10⁻⁵m，对甲酸的表观米氏常数为2.2×10⁻⁴m。该酶在约60℃以及pH值在7.0至9.0之间时活性最高。该酶催化¹⁴CO₂与甲酸之间的交换反应，此反应需要NADP，但无法证明能从CO₂和还原型烟酰胺腺嘌呤二核苷酸磷酸净合成甲酸。该反应不涉及铁氧化还原蛋白。
