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


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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.

作者简介

I. Shelaev

Semenov Institute of Chemical Physics

Email: b.dzhagarov@ifanbel.bas-net.by
俄罗斯联邦, Moscow, 119991

F. Gostev

Semenov Institute of Chemical Physics

Email: b.dzhagarov@ifanbel.bas-net.by
俄罗斯联邦, Moscow, 119991

T. Vygodina

Belozerski Institute of Physicochemical Biology

Email: b.dzhagarov@ifanbel.bas-net.by
俄罗斯联邦, Moscow, 119991

S. Lepeshkevich

Stepanov Institute of Physics

Email: b.dzhagarov@ifanbel.bas-net.by
白俄罗斯, Minsk, 220072

B. Dzhagarov

Stepanov Institute of Physics

编辑信件的主要联系方式.
Email: b.dzhagarov@ifanbel.bas-net.by
白俄罗斯, Minsk, 220072

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