scholarly journals Electron paramagnetic resonance studies on membrane-bound respiratory nitrate reductase ofKlebsiella aerogenes

FEBS Letters ◽  
1978 ◽  
Vol 90 (1) ◽  
pp. 107-111 ◽  
Author(s):  
H.J. Bosma ◽  
R. Wever ◽  
J. Van 't Riet
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Nitrate Reductase ◽  
Paramagnetic Resonance ◽  
Membrane Bound ◽  
Electron Paramagnetic ◽  
Respiratory Nitrate Reductase

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

1976 ◽  
Vol 155 (1) ◽  
pp. 201-203 ◽  
Author(s):  
R C Bray ◽  
S P Vincent ◽  
D J Lowe ◽  
R A Clegg ◽  
P B Garland
Keyword(s):  
Escherichia Coli ◽  
Electron Paramagnetic Resonance ◽  
Nitrate Reductase ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Resonance Spectroscopy ◽  
Paramagnetic Resonance ◽  
Escherichia Coli K12 ◽  
Electron Paramagnetic ◽  
Respiratory Nitrate Reductase

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.

scholarly journals Investigation by electron paramagnetic resonance spectroscopy of the molybdenum centre of respiratory nitrate reductase from Paracoccus denitrificans

1988 ◽  
Vol 252 (3) ◽  
pp. 925-926 ◽  
Author(s):  
N Turner ◽  
A L Ballard ◽  
R C Bray ◽  
S Ferguson
Keyword(s):  
Escherichia Coli ◽  
Nitrate Reductase ◽  
Paracoccus Denitrificans ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Resonance Spectroscopy ◽  
Species Comparison ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic ◽  
Respiratory Nitrate Reductase ◽  
Active Centres

The molybdenum centre of respiratory nitrate reductase from Paracoccus denitrificans has been investigated by e.p.r. spectroscopy of Mo(V). In common with the centres of the analogous enzymes from Escherichia coli and Pseudomonas aeruginosa, it undergoes a pH- and anion-dependent transition between two different e.p.r. signal-giving species. Comparison of the relevant e.p.r. parameters extracted with the help of computer simulations reveals ligation of the metal in the active centres of the three enzymes to be identical.

scholarly journals Particulate methane monooxygenase contains only mononuclear copper centers

Science ◽  
2019 ◽  
Vol 364 (6440) ◽  
pp. 566-570 ◽  
Author(s):  
Matthew O. Ross ◽  
Fraser MacMillan ◽  
Jingzhou Wang ◽  
Alex Nisthal ◽  
Thomas J. Lawton ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Methane Oxidation ◽  
Active Site ◽  
Methane Monooxygenase ◽  
Spectroscopic Characterization ◽  
Metabolic Enzyme ◽  
Particulate Methane Monooxygenase ◽  
Paramagnetic Resonance ◽  
Membrane Bound ◽  
Electron Paramagnetic

Bacteria that oxidize methane to methanol are central to mitigating emissions of methane, a potent greenhouse gas. The nature of the copper active site in the primary metabolic enzyme of these bacteria, particulate methane monooxygenase (pMMO), has been controversial owing to seemingly contradictory biochemical, spectroscopic, and crystallographic results. We present biochemical and electron paramagnetic resonance spectroscopic characterization most consistent with two monocopper sites within pMMO: one in the soluble PmoB subunit at the previously assigned active site (CuB) and one ~2 nanometers away in the membrane-bound PmoC subunit (CuC). On the basis of these results, we propose that a monocopper site is able to catalyze methane oxidation in pMMO.

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