Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin

被引：589

作者：

Collman, JP ^{[1
]}

Boulatov, R ^{[1
]}

Sunderland, CJ ^{[1
]}

Fu, L ^{[1
]}

机构：

[1] Stanford Univ, Dept Chem, Stanford, CA 94305 USA

来源：

CHEMICAL REVIEWS | 2004年 / 104卷 / 02期

关键词：

D O I：

10.1021/cr0206059

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Functional analogues of cytochrome c oxidase, myoglobin (Mb) and hemoglobin (Hb) were studied. Quantitative correlation between the properties of the O 2-binding pocket and the O 2 affinity of the heme were also investigated. The results show the minimum stereoelectronic requirements for reversible oxygenation of ferroheme. It was also found that embedding ferroheme in a sufficiently large hydrophobic envelope allows reversible O 2 binding, even in protic media.

引用

页码：561 / 588

页数：28

共 173 条

[1]

Abramson J, 2000, NAT STRUCT BIOL, V7, P910

[2] Structure of cytochrome c oxidase:: a comparison of the bacterial and mitochondrial enzymes [J].