THE PATHWAY OF CO BINDING TO CYTOCHROME-C-OXIDASE - CAN THE GATEWAY BE CLOSED

被引：14

作者：

HILL, BC

机构：

[1] Department of Biochemistry, Queen's University, Kingston

来源：

FEBS LETTERS | 1994年 / 354卷 / 03期

关键词：

CYTOCHROME C OXIDASE; LIGAND BINDING; BINUCLEAR CENTER; CYTOCHROME ALPHA(3)-CU-B; CYANIDE; CARBON MONOXIDE;

D O I：

10.1016/0014-5793(94)01140-0

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：

Addition of cyanide to the CO complex of cytochrome oxidase reduces the apparent photosensitivity of the Fe-CO bond. This effect is not seen with azide, or when cyanide is added to ferromyoglobin-CO. It is proposed that cyanide binds to Cu-B, and restricts the passage of CO out of the protein. This restriction favors geminate recombination of CO and ferrocytochrome a,, thereby lowering the apparent quantum yield for CO photolysis. The apparent K-d of cyanide for Cu-B is 15.4 mM. These data support a direct role for Cu-B in ligand binding by cytochrome c oxidase.

引用

收藏

页码：284 / 288

页数：5

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