在以含钼培养基培养的假单胞菌属101细胞中存在一种新的依赖NAD⁺的甲酸脱氢酶的证据。

Evidence for the presence of a new NAD+-dependent formate dehydrogenase in Pseudomonas sp. 101 cells grown on a molybdenum-containing medium.

作者信息

Karzanov V V, Tishkov V I, Egorov A M

机构信息

Chemistry Department, M.V. Lomonosov State University, Moscow, U.S.S.R.

出版信息

FEMS Microbiol Lett. 1989 Jul 15;51(1):197-200. doi: 10.1016/0378-1097(89)90508-9.

DOI:10.1016/0378-1097(89)90508-9

PMID:2777065

Abstract

The facultatively methylotrophic bacterium Pseudomonas sp. 101, grown on methanol in presence of molybdate, contains a new formate dehydrogenase (N-FDH) catalyzing NAD+-dependent oxidation of formate. The activity of this N-FDH could also be measured in presence of artificial electron acceptors, ferricyanide and 2,6-dichlorophenol indophenol. This new enzyme is absent in cells grown on a methanol-containing medium with tungstate, where only another two, previously described formate dehydrogenases, which are active only with NAD+ or only with artificial acceptors, respectively, were determined. The N-FDH was partially purified by a combination of ion-exchange and gel-filtration chromatography, and was shown to differ in its properties from the known NAD+-dependent counterpart.

摘要

兼性甲基营养细菌假单胞菌属101在钼酸盐存在下于甲醇上生长时，含有一种新型甲酸脱氢酶（N-FDH），可催化NAD⁺依赖性的甲酸氧化反应。该N-FDH的活性也可在人工电子受体铁氰化物和2,6-二氯酚靛酚存在的情况下进行测定。在含有钨酸盐的甲醇培养基上生长的细胞中不存在这种新酶，在该培养基中仅测定到另外两种先前描述的甲酸脱氢酶，它们分别仅对NAD⁺或仅对人工受体有活性。通过离子交换和凝胶过滤色谱相结合的方法对N-FDH进行了部分纯化，结果表明其性质与已知的NAD⁺依赖性对应物不同。