氧气与完全还原型细胞色素c氧化酶反应的主要中间体。
Primary intermediate in the reaction of oxygen with fully reduced cytochrome c oxidase.
作者信息
Han S W, Ching Y C, Rousseau D L
机构信息
AT&T Bell Laboratories, Murray Hill, NJ 07974.
出版信息
Proc Natl Acad Sci U S A. 1990 Apr;87(7):2491-5. doi: 10.1073/pnas.87.7.2491.
Abstract
The primary intermediate in the reaction of oxygen with cytochrome c oxidase was generated by photodissociating carbon monoxide in a continuous flow rapid mixing apparatus. The presence of the primary intermediate was confirmed by a comparison of the iron-dioxygen stretching frequency with that obtained in the reaction of oxygen with the mixed-valence enzyme. For both of these preparations, the Fe-O2 stretching mode is detected at 568 cm-1, the same frequency as that found in oxyhemoglobin and oxymyoglobin. These data illustrate that the primary intermediate may be generated and detected at room temperature in the fully reduced enzyme and that the oxidation state of cytochrome a does not affect the structure of the iron-dioxygen complex. By following the changes in the intensity of the Fe-O2 stretching mode in the resonance Raman spectrum as a function of time, the first-order rate constant for the decay of the primary intermediate was found to be 3.5 x 10(4) s-1 (t1/2 = 20 microseconds).
摘要
在连续流动快速混合装置中，通过光解离一氧化碳生成了氧气与细胞色素c氧化酶反应的主要中间体。通过将铁-双氧伸缩频率与氧气与混合价态酶反应中获得的频率进行比较，证实了主要中间体的存在。对于这两种制剂，在568 cm-1处检测到Fe-O2伸缩模式，与在氧合血红蛋白和肌红蛋白中发现的频率相同。这些数据表明，主要中间体可以在室温下在完全还原的酶中产生和检测到，并且细胞色素a的氧化态不影响铁-双氧配合物的结构。通过跟踪共振拉曼光谱中Fe-O2伸缩模式强度随时间的变化，发现主要中间体衰变的一级速率常数为3.5×10(4) s-1（t1/2 = 20微秒）。
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本文引用的文献
1
Reactions of cytochrome oxidase with oxygen and carbon monoxide.细胞色素氧化酶与氧气和一氧化碳的反应。
Biochem J. 1963 Mar;86(3):541-54. doi: 10.1042/bj0860541.
2
Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance raman scattering.通过共振拉曼散射研究脱氧血红蛋白和氧合血红蛋白血红素的四级结构及低频分子振动。
J Mol Biol. 1980 Jan 25;136(3):271-89. doi: 10.1016/0022-2836(80)90374-5.
3
A re-examination of the reactions of cyanide with cytochrome c oxidase.氰化物与细胞色素c氧化酶反应的重新审视。
Biochem J. 1984 May 15;220(1):57-66. doi: 10.1042/bj2200057.
4
Formation and decay of the primary oxygen compound of cytochrome oxidase at room temperature as observed by stopped flow, laser flash photolysis and rapid scanning.
J Biol Chem. 1984 Jun 10;259(11):7187-90.
5
The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature. Evidence for new pathways of electron transfer.在室温下通过流动闪光分光光度法研究完全还原的细胞色素c氧化酶与氧气的反应。电子转移新途径的证据。
Biochem J. 1984 Mar 15;218(3):913-21. doi: 10.1042/bj2180913.
6
Spectroscopic evidence for the participation of compound A (Fea32+-O2) in the reaction of mixed-valence cytochrome c oxidase with oxygen at room temperature.化合物A（Fea32+-O2）在室温下参与混合价态细胞色素c氧化酶与氧气反应的光谱学证据。
Biochem J. 1983 Dec 1;215(3):659-67. doi: 10.1042/bj2150659.
7
Cyanide inhibition of cytochrome c oxidase. A rapid-freeze e.p.r. investigation.氰化物对细胞色素c氧化酶的抑制作用。快速冷冻电子顺磁共振研究。
Biochem J. 1984 Dec 15;224(3):829-37. doi: 10.1042/bj2240829.
8
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。
Biochim Biophys Acta. 1972 Feb 28;256(2):258-76. doi: 10.1016/0005-2728(72)90057-6.
9
Biochemical and biophysical studies on cytochrome aa 3 . V. Binding of cyanide to cytochrome aa 3 .细胞色素aa3的生化与生物物理研究。V. 氰化物与细胞色素aa3的结合。
Biochim Biophys Acta. 1972 Feb 28;256(2):243-57. doi: 10.1016/0005-2728(72)90056-4.
10
The reaction of reduced cytochrome C oxidase with oxygen.还原型细胞色素C氧化酶与氧气的反应。
J Biol Chem. 1967 Apr 25;242(8):1782-7.
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