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 Lettjournal_title
FEBS lettersauthors
Dennison C,Berg A,de Vries S,Canters GWdoi
10.1016/0014-5793(96)00981-7subject
Has Abstractpub_date
1996-10-07 00:00:00pages
340-4issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00981-7journal_volume
394pub_type
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