1H NMR studies of the paramagnetic CuAcenter 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 H-1 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.
