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J Chem Phys. 2010 Mar 21;132(11):115105. doi: 10.1063/1.3356027.
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A two-layer gold surface with improved surface enhancement for spectro-electrochemistry using surface-enhanced infrared absorption spectroscopy.一种具有改进表面增强功能的双层金表面,用于采用表面增强红外吸收光谱的光谱电化学。
Appl Spectrosc. 2009 Sep;63(9):1068-74. doi: 10.1366/000370209789379330.
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Monitoring the redox and protonation dependent contributions of cardiolipin in electrochemically induced FTIR difference spectra of the cytochrome bc(1) complex from yeast.监测酵母细胞色素bc(1)复合物电化学诱导傅里叶变换红外差谱中的心磷脂的氧化还原和质子化依赖性贡献。
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Redox-dependent conformational changes in cytochrome C oxidase suggest a gating mechanism for proton uptake.细胞色素C氧化酶中依赖氧化还原的构象变化表明了质子摄取的门控机制。
Biochemistry. 2009 Jun 16;48(23):5121-30. doi: 10.1021/bi9001387.
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High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: new insights into the active site and the proton transfer pathways.反硝化副球菌细胞色素c氧化酶的高分辨率晶体结构:对活性位点和质子转移途径的新见解
Biochim Biophys Acta. 2009 Jun;1787(6):635-45. doi: 10.1016/j.bbabio.2009.04.003. Epub 2009 Apr 15.
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A peroxide bridge between Fe and Cu ions in the O2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump.在完全氧化的细胞色素c氧化酶的O2还原位点中,铁离子和铜离子之间的过氧化物桥可能会抑制质子泵。
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Analysis of the electrochemistry of hemes with E(m)s spanning 800 mV.对氧化还原电位跨度为800毫伏的血红素的电化学分析。
Proteins. 2009 May 15;75(3):719-34. doi: 10.1002/prot.22282.
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Cytochrome c oxidase: exciting progress and remaining mysteries.细胞色素c氧化酶:令人振奋的进展与未解之谜
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Spectroscopic study on the communication between a heme a3 propionate, Asp399 and the binuclear center of cytochrome c oxidase from Paracoccus denitrificans.
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二维二次离子共振光谱学突出了直接电子转移诱导的细胞色素 c 氧化酶构象变化。

2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer.

机构信息

Austrian Institute of Technology GmbH, AIT, Donau-City Str. 1, 1220 Vienna, Austria.

出版信息

Metallomics. 2011 Jun;3(6):619-27. doi: 10.1039/c0mt00083c. Epub 2011 May 4.

DOI:10.1039/c0mt00083c
PMID:21541411
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3912184/
Abstract

Potentiometric titrations of the cytochrome c oxidase (CcO) immobilized in a biomimetic membrane system were followed by two-dimensional surface-enhanced IR absorption spectroscopy (2D SEIRAS) in the ATR-mode. Direct electron transfer was employed to vary the redox state of the enzyme. The CcO was shown to undergo a conformational transition from a non-activated to an activated state after it was allowed to turnover in the presence of oxygen. Differences between the non-activated and activated state were revealed by 2D SEIRA spectra recorded as a function of potential. The activated state was characterized by a higher number of correlated transitions as well as a higher number of amino acids associated with electron transfer.

摘要

采用二维表面增强红外吸收光谱(2D SEIRAS)在衰减全反射(ATR)模式下对固定在仿生膜系统中的细胞色素 c 氧化酶(CcO)进行了电位滴定。直接电子转移用于改变酶的氧化还原状态。结果表明,CcO 在有氧存在的情况下发生周转后,会从非激活状态转变为激活状态。通过记录作为电位函数的二维 SEIRA 光谱,可以揭示非激活状态和激活状态之间的差异。激活状态的特点是相关跃迁的数量增加,以及与电子转移相关的氨基酸数量增加。