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.
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.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.