H-1 NMR studies of the paramagnetic Cu-A center of cytochrome oxidase

被引：36

作者：

Dennison, C

Berg, A

deVries, S

Canters, GW

机构：

[1] LEIDEN UNIV,GORLAEUS LABS,INST CHEM,NL-2300 RA LEIDEN,NETHERLANDS

[2] TECH UNIV DELFT,DEPT MICROBIOL & ENZYMOL,NL-2628 BC DELFT,NETHERLANDS

来源：

FEBS LETTERS | 1996年 / 394卷 / 03期

关键词：

copper protein; amicyanin; paramagnetic NMR; cytochrome c oxidase;

D O I：

10.1016/0014-5793(96)00981-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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收藏

页码：340 / 344

页数：5

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