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1 H NMR studies of the paramagnetic Cu A center of cytochrome oxidase
Author(s) -
Dennison Christopher,
Berg Axel,
de Vries Simon,
Canters Gerard W.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00981-7
Subject(s) - cytochrome c oxidase , paramagnetism , chemistry , oxidase test , crystallography , cytochrome , electron transport complex iv , nuclear magnetic resonance , stereochemistry , enzyme , biochemistry , physics , quantum mechanics
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.