Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin

被引：584
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.
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页码：561 / 588
页数：28
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