Time-Resolved Surface-Enhanced IR-Absorption Spectroscopy of Direct Electron Transfer to Cytochrome c Oxidase from R. sphaeroides

被引：17
作者：
Schwaighofer, Andreas [1 ]
Steininger, Christoph [1 ]
Hildenbrandt, David M. [1 ]
Srajer, Johannes [1 ,2 ]
Nowak, Christoph [1 ,2 ]
Knoll, Wolfgang [1 ]
Naumann, Renate L. C. [1 ]
机构：
[1] Austrian Inst Technol, Vienna, Austria
[2] Ctr Electrochem Surface Technol, Wiener Neustadt, Austria
来源：
BIOPHYSICAL JOURNAL | 2013年 / 105卷 / 12期
关键词：
ACTIVE-SITE; PARACOCCUS-DENITRIFICANS; INFRARED-SPECTROSCOPY; HIS-TYR; HEME; MEMBRANE; PROTEIN; FTIR; SPECTROELECTROCHEMISTRY; BINDING;
D O I：
10.1016/j.bpj.2013.10.037
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
Time-resolved surface-enhanced IR-absorption spectroscopy triggered by electrochemical modulation has been performed on cytochrome c oxidase from Rhodobacter sphaeroides. Single bands isolated from a broad band in the amide I region using phase-sensitive detection were attributed to different redox centers. Their absorbances changing on the millisecond timescale could be fitted to a model based on protonation-dependent chemical reaction kinetics established previously. Substantial conformational changes of secondary structures coupled to redox transitions were revealed.
引用
收藏
页码：2706 / 2713
页数：8
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