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. 1976 Apr 1;155(1):201–203. doi: 10.1042/bj1550201

Electron-paramagnetic-resonance studies on the molybdenum of nitrate reductase from Escherichia coli K12.

R C Bray, S P Vincent, D J Lowe, R A Clegg, P B Garland
PMCID: PMC1172819  PMID: 180982

Abstract

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.

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Selected References

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