Rodionov Iu V, Zakharova E V
Biokhimiia. 1980 May;45(5):854-63.
The cells of Achromobacter parvulus, strain 1T, when grown in a methanol-containing medium, have two formate dehydrogenases, i.e. NAD-linked formate dehydrogenase and the formate dehydrogenase reducing the ferricyanide and tetrazolia. Only the latter enzyme was found in the cells grown in a medium with glycerol as a carbon source. These enzymes differ with respect to Km for formate and antigenic specificity. Km for formate oxidation by the cells of A. parvulus is lower than for formate of the NAD-dependent formate dehydrogenase and is equal to Km for the enzyme reducing artificial electron acceptors. The results obtained are discussed in terms of the existence of two cytochrome oxidase systems in the methylotrophic bacteria, differing in their sensitivities to the inhibition by formate.
细小无色杆菌1T菌株的细胞在含甲醇的培养基中生长时，有两种甲酸脱氢酶，即NAD连接的甲酸脱氢酶和还原铁氰化物及四氮唑的甲酸脱氢酶。在以甘油作为碳源的培养基中生长的细胞中，仅发现了后一种酶。这些酶在甲酸的米氏常数（Km）和抗原特异性方面存在差异。细小无色杆菌细胞氧化甲酸的Km低于NAD依赖性甲酸脱氢酶的甲酸Km，且等于还原人工电子受体的酶的Km。根据甲基营养细菌中存在两种对甲酸抑制敏感性不同的细胞色素氧化酶系统，对所得结果进行了讨论。
