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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Dennison C,Berg A,de Vries S,Canters GW

doi

10.1016/0014-5793(96)00981-7

subject

Has Abstract

pub_date

1996-10-07 00:00:00

pages

340-4

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00981-7

journal_volume

394

pub_type

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