Investigation by electron paramagnetic resonance spectroscopy of the molybdenum centre of respiratory nitrate reductase from Paracoccus denitrificans.
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.
Turner
N
N
School of Chemistry and Molecular Sciences, University of Sussex, Brighton, U.K.
Ballard
A L
AL
Bray
R C
RC
Ferguson
S
S
D004578:Electron Spin Resonance Spectroscopy; D008982:Molybdenum / Q000032:analysis*; D050901:Nitrate Reductase; D009565:Nitrate Reductases; D010231:Paracoccus denitrificans / Q000201:enzymology*
D008982:Molybdenum; D009565:Nitrate Reductases; D050901:Nitrate Reductase