THE SITE OF THE REDOX-LINKED PROTON PUMP IN EUKARYOTIC CYTOCHROME-C OXIDASES

被引：4

作者：

HOLM, DE

GODETTE, G

BONAVENTURA, J

BONAVENTURA, C

PETERSON, J

机构：

[1] UNIV ALABAMA, DEPT CHEM, TUSCALOOSA, AL 35487 USA

[2] DUKE UNIV, MARINE LAB, CTR MARINE BIOMED, BEAUFORT, NC 28516 USA

来源：

FEBS LETTERS | 1995年 / 370卷 / 1-2期

关键词：

CYTOCHROME OXIDASE; EPR; MCD; PROTON PUMP; SHARK;

D O I：

10.1016/0014-5793(95)00791-7

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 electronic spectra of fully oxidized derivatives of some cytochrome c oxidase preparations are distinctly pH dependent, In general, the observed spectral shifts are greater in the case of pulsed derivatives compared to resting preparations and also, greater for preparations of the enzyme from shark skeletal muscle compared to beef heart. The low temperature near-infrared magnetic circular dichroism spectrum of the fully oxidized shark enzyme is not pH dependent in the experimental range, indicating the sensitivity of the visible region electronic spectrum to variation in pH to be due principally to changes at the heme a(3)-Cu-B chromophore, The results are discussed in relation to proposed mechanisms of proton translocation in cytochrome c oxidase.

引用

页码：53 / 58

页数：6

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