Femtosecond absorption spectroscopy of cytochrome c oxidase: Excited electronic states and relaxation processes in heme a and heme a 3 centers

被引：3
|
作者：
Shelaev, I. V. [1 ]
Gostev, F. E. [1 ]
Vygodina, T. V. [2 ]
Lepeshkevich, S. V. [3 ]
Dzhagarov, B. M. [3 ]
机构：
[1] Russian Acad Sci, Semenov Inst Chem Phys, Moscow 119991, Russia
[2] Moscow MV Lomonosov State Univ, Belozerski Inst Physicochem Biol, Moscow 119991, Russia
[3] Natl Acad Sci Belarus, Stepanov Inst Phys, Minsk 220072, BELARUS
来源：
HIGH ENERGY CHEMISTRY | 2018年 / 52卷 / 01期
基金：
俄罗斯基础研究基金会;
关键词：
cytochrome c oxidase; femtosecond absorption spectroscopy; excited electronic states; relaxation processes; spectral transient species; OPTICAL-PROPERTIES; DYNAMICS; MYOGLOBIN; BINDING;
D O I：
10.1134/S0018143918010101
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
Cytochrome c oxidase, the key bioenergetic protein, was studied by femtosecond absorption spectroscopy. Time-resolved spectral characteristics of the difference spectra recorded in the timescale from 80 fs to 20 ps were analyzed. Electronic relaxation of the excitation energy in heme a occurs in three successive steps. After completion of these steps, heme a is in the excited vibrational state of the ground state. Vibrational relaxation, cooling of the heme, occurs for several picoseconds.
引用
收藏
页码：45 / 51
页数：7
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