Femtosecond absorption spectroscopy of cytochrome c oxidase: Excited electronic states and relaxation processes in heme a and heme a3 centers


Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription Access

Abstract

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.

About the authors

I. V. Shelaev

Semenov Institute of Chemical Physics

Email: b.dzhagarov@ifanbel.bas-net.by
Russian Federation, Moscow, 119991

F. E. Gostev

Semenov Institute of Chemical Physics

Email: b.dzhagarov@ifanbel.bas-net.by
Russian Federation, Moscow, 119991

T. V. Vygodina

Belozerski Institute of Physicochemical Biology

Email: b.dzhagarov@ifanbel.bas-net.by
Russian Federation, Moscow, 119991

S. V. Lepeshkevich

Stepanov Institute of Physics

Email: b.dzhagarov@ifanbel.bas-net.by
Belarus, Minsk, 220072

B. M. Dzhagarov

Stepanov Institute of Physics

Author for correspondence.
Email: b.dzhagarov@ifanbel.bas-net.by
Belarus, Minsk, 220072

Supplementary files

Supplementary Files
Action
1. JATS XML

Copyright (c) 2018 Pleiades Publishing, Ltd.