Evidence for the presence of a new NAD+-dependent formate dehydrogenase in Pseudomonas sp. 101 cells grown on a molybdenum-containing medium.
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.
Chemistry Department, M.V. Lomonosov State University, Moscow, U.S.S.R.
V V
VV
Karzanov
Bogatsky YuA
V I
VI
Tishkov
A M
AM
Egorov
D000445:Aldehyde Oxidoreductases / Q000302:isolation & purification*; D003470:Culture Media / Q000378:metabolism; D005560:Formate Dehydrogenases / Q000302:isolation & purification* / Q000378:metabolism; D000432:Methanol / Q000378:metabolism; D008982:Molybdenum / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology*
D003470:Culture Media; D009243:NAD; C044659:molybdate; D008982:Molybdenum; D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases; D000432:Methanol