1H NMR studies of the paramagnetic CuA center of cytochrome oxidase

Abstract The dinuclear paramagnetic center of the soluble Cu A domain of the cytochrome c oxidase from Bacillus subtilis has been studied using 1 H NMR. The spectrum possesses remarkably sharp shifted resonances. Comparison with the spectrum of the Cu A amicyanin variant provides the spin density distribution in the Cu A site of cytochrome c oxidase. This represents the first paramagnetic NMR study of the dinuclear Cu A center from the soluble domain of subunit II of cytochrome c oxidase.