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• W2016427706 abstract "The assimilatory nitrate reductase from the phototrophic bacterium Rhodobacter capsulatus has been purified to electrophoretic homogeneity and its molecular and kinetic parameters determined. The native nitrate reductase is a dimer of 144 kDa composed of two subunits of 46 and 95 kDa. The purified enzyme catalyzes the electron transfer from NADH, reduced bromophenol blue or reduced viologens to nitrate. The nitrate reductase contains 1 mol FAD per mole of enzyme and also reduces cytochrome c or dichlorophenol indophenol with NADH as the electron donor. The diaphorase activity is located in the small subunit." @default.
• W2016427706 created "2016-06-24" @default.
• W2016427706 creator A5053410178 @default.
• W2016427706 creator A5086153388 @default.
• W2016427706 creator A5086703553 @default.
• W2016427706 date "1997-09-01" @default.
• W2016427706 modified "2023-10-17" @default.
• W2016427706 title "The assimilatory nitrate reductase from the phototrophic bacterium,Rhodobacter capsulatusE1F1, is a flavoprotein" @default.
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• W2016427706 doi "https://doi.org/10.1016/s0014-5793(97)00968-x" @default.
• W2016427706 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9305729" @default.
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