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

15 July 1989

journal article
Published by Oxford University Press (OUP) in FEMS Microbiology Letters

Vol. 60 (2) , 197-200
https://doi.org/10.1016/0378-1097(89)90508-9

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.

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