1H NMR studies of the paramagnetic CuA center of cytochrome oxidase.
The dinuclear paramagnetic center of the soluble CuA domain of the cytochrome c oxidase from Bacillus subtilis has been studied using 1H NMR. The spectrum possesses remarkably sharp shifted resonances. Comparison with the spectrum of the CuA amicyanin variant provides the spin density distribution in the CuA site of cytochrome c oxidase. This represents the first paramagnetic NMR study of the dinuclear CuA center from the soluble domain of subunit II of cytochrome c oxidase.
Dennison
C
C
Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, The Netherlands.
Berg
A
A
de Vries
S
S
Canters
G W
GW
D001412:Bacillus subtilis / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins / Q000737:chemistry*; D009154:Mutation; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D008667:Metalloproteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; C017079:mauC protein, Methylobacterium extorquens; D003300:Copper; D003576:Electron Transport Complex IV