Electron-paramagnetic-resonance studies on the molybdenum of nitrate reductase from Escherichia coli K12.
Studies on the respiratory nitrate reductase (EC 1.7.99.4) from Escherichia coli K12 by electron-paramagnetic-resonance spectroscopy indicate that its molybdenum centre is comparable with that in other molybdenum-containing enzymes. Two Mo(V) signals may be observed; one shows interaction of Mo(V) with a proton exchangeable with the solvent and has: A (1H) 0.9-1.2mT; g1 = 1.999; g2=1.985; g3 = 1.964; gav. = 1.983. Molybdenum of both signal-giving species may be reduced with dithionite and reoxidized with nitrate.
D004578:Electron Spin Resonance Spectroscopy; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D008982:Molybdenum / Q000032:analysis*; D009565:Nitrate Reductases / Q000032:analysis* / Q000302:isolation & purification; D012967:Sodium Dodecyl Sulfate
D012967:Sodium Dodecyl Sulfate; D008982:Molybdenum; D009565:Nitrate Reductases