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细胞色素c氧化酶化学的当前问题。

Current issues in the chemistry of cytochrome c oxidase.

作者信息

Palmer G

机构信息

Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251-1892.

出版信息

J Bioenerg Biomembr. 1993 Apr;25(2):145-51. doi: 10.1007/BF00762856.

DOI:10.1007/BF00762856
PMID:8389747
Abstract

Some contemporary issues relevant to the chemistry of mammalian cytochrome c oxidase are discussed. These include the optical properties of heme A and the spectroscopic consequences of the differences in side-chain substitution compared to heme B; a common fallacy concerning the electrostatic exchange interaction between cytochrome a3 and CuB; the question of the number and location of the copper components of the enzyme; and the mode of binding of ligands such as cyanide and azide.

摘要

讨论了一些与哺乳动物细胞色素c氧化酶化学相关的当代问题。这些问题包括血红素A的光学性质以及与血红素B相比侧链取代差异的光谱学后果;关于细胞色素a3和CuB之间静电交换相互作用的一个常见错误观念;该酶铜组分的数量和位置问题;以及氰化物和叠氮化物等配体的结合模式。

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1
Current issues in the chemistry of cytochrome c oxidase.细胞色素c氧化酶化学的当前问题。
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2
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3
Infrared and EPR studies on cyanide binding to the heme-copper binuclear center of cytochrome bo-type ubiquinol oxidase from Escherichia coli. Release of a CuB-cyano complex in the partially reduced state.关于氰化物与大肠杆菌细胞色素bo型泛醇氧化酶的血红素-铜双核中心结合的红外和电子顺磁共振研究。部分还原状态下CuB-氰配合物的释放。
J Biol Chem. 1996 Feb 23;271(8):4017-22. doi: 10.1074/jbc.271.8.4017.
4
Distal Cu ion protects synthetic heme/Cu analogues of cytochrome oxidase against inhibition by CO and cyanide.远端铜离子可保护细胞色素氧化酶的合成血红素/铜类似物免受一氧化碳和氰化物的抑制。
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Exclusive CO binding to cytochrome oxidase.一氧化碳与细胞色素氧化酶的特异性结合。
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6
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Cyanide inhibition and pyruvate-induced recovery of cytochrome c oxidase.氰化物抑制和丙酮酸诱导的细胞色素 c 氧化酶的恢复。
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本文引用的文献

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Magnetization of fast and slow oxidized cytochrome c oxidase.快速和慢速氧化细胞色素c氧化酶的磁化
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Models of the two heme centers in cytochrome oxidase. The optical properties of cytochrome a and a3.细胞色素氧化酶中两个血红素中心的模型。细胞色素a和a3的光学性质。
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对一种模拟细胞色素C氧化酶酪氨酸-组氨酸交联的三齿铜配合物的光谱研究。
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Biochemical and biophysical studies on cytochrome c oxidase. XI. Reaction with azide.细胞色素c氧化酶的生化与生物物理研究。XI. 与叠氮化物的反应。
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Biochemical and biophysical studies on cytochrome aa 3 . 8. Effect of cyanide on the catalytic activity.细胞色素aa3的生化与生物物理研究。8. 氰化物对催化活性的影响。
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Biochemical and biophysical studies on cytochrome aa 3 . VI. Reaction of cyanide with oxidized and reduced enzyme.细胞色素aa3的生化与生物物理研究。VI. 氰化物与氧化型和还原型酶的反应。
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The stoichiometry and absorption spectra of components a and a-3 in cytochrome c oxidase.细胞色素c氧化酶中组分a和a-3的化学计量学及吸收光谱。
Biochemistry. 1966 Mar;5(3):838-48. doi: 10.1021/bi00867a005.
8
The reaction of cytochrome oxidase with cyanide. Preparation of the rapidly reacting form and its conversion to the slowly reacting form.细胞色素氧化酶与氰化物的反应。快速反应形式的制备及其向缓慢反应形式的转化。
J Biol Chem. 1987 Jan 15;262(2):595-604.
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Analysis of the Cu, Fe, and Zn contents in cytochrome C oxidases from different species and tissues by proton-induced X-ray emission (PIXE).
Biochem Biophys Res Commun. 1986 Nov 14;140(3):1007-14. doi: 10.1016/0006-291x(86)90735-7.
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The structure of the cytochrome a3-CuB site of mammalian cytochrome c oxidase as probed by MCD and EPR spectroscopy.通过磁圆二色光谱和电子顺磁共振光谱探测的哺乳动物细胞色素c氧化酶的细胞色素a3-CuB位点结构。
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