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PMID: 180982 Published · ppublish English Journal Article

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

The Biochemical journal ·Vol. 155 ·No. 1 ·1976-04-01 ·Pages 201-3

Bray RC, Vincent SP, Lowe DJ, Clegg RA, Garland PB

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.

MeSH Terms
Electron Spin Resonance Spectroscopy Electrophoresis, Polyacrylamide Gel Escherichia coli/enzymology Molybdenum/analysis Nitrate Reductases/analysis,isolation & purification Sodium Dodecyl Sulfate
Chemicals
Sodium Dodecyl Sulfate Molybdenum Nitrate Reductases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Bray R C
Vincent S P
Lowe D J
Clegg R A
Garland P B
References (17)
17 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1976-04-01
Pages
201-3
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1172819
Subset
IM
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