ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1989.tb03445.x
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