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- W1977068968 abstract "A particulate nitrate reductase has been prepared from actively denitrifying cells of Pseudomonas denitrificans. The enzyme system which utilizes formate as an electron donor and contains flavin, sulphydryl groups and a metallic component(s) reduces NO3− stoichiometrically to NO2−. Actively growing cells and resting cell suspensions reduced NO2− mainly to N2, but small amounts of NO and N2O were also produced. ClO3− and BrO3− which were competitive inhibitors of NO3− reduction also served as electron acceptors for formate dehydrogenase. The particulate nitrate reductase which was associated with the respiratory chain was solubilized by deoxycholate treatment and purified about 60-fold. The purified enzyme which has a cytochrome b-type absorption spectrum utilized reduced dyes such as benzylviologen as an electron donor, but was no longer active with the natural donors, formate and NADH. Horse heart cytochrome c reduced with ascorbate-tetramethylphenylenediamine did not serve as an electron donor. Metal chelating agents, especially those that bind molybdenum (dithiol and KCNS), and the sulfhydryl groups reagent p-chloromercuribenzoate were highly inhibitory." @default.
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- W1977068968 date "1970-05-01" @default.
- W1977068968 modified "2023-09-27" @default.
- W1977068968 title "Some properties of a nitrate reductase from Pseudomonas denitrificans" @default.
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- W1977068968 doi "https://doi.org/10.1016/0005-2728(70)90257-4" @default.
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