|
ИСТИНА |
Войти в систему Регистрация |
ИПМех РАН |
||
Femtosecond absorption spectroscopy of reduced and oxidized forms of cytochrome c oxidase: excited states and relaxation processes in heme a and a3 centersстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Дата последнего поиска статьи во внешних источниках: 24 января 2020 г.
- Авторы: Shelaev I.V., Gostev F.E., Vygodina T.V., Lepeshkevich S.V., Dzhagarov B.M.
- Журнал: Optics and Spectroscopy (English translation of Optika i Spektroskopiya), издательство Optical Society of America (United States)
- Том: 127
- Номер: 4
- Год издания: 2019
- Первая страница: 756
- Последняя страница: 762
- DOI: 10.1134/S0030400X19100278
- Аннотация: Excited electronic states and intraheme relaxation processes in the oxidized and reduced forms of mitochondrial cytochrome c oxidase from bovine cardiac muscle have been investigated by femtoseconds absorption spectroscopy. The spectral and kinetic characteristics of short-lived intermediates have been measured from 80 fs to 20 ps after photoexcitation. It is found that nonradiative electron relaxation of the excitation energy in heme a, both in the oxidized (FeIII a) and rediced (FeII a) forms occurs successively as three processes, after the end of which heme a is in the ground state with a large store of vibrational energy. The subsequent vibrational relaxation (heme cooling) lasts for several picoseconds. It is found for reduced heme a3 (FeII a3) that the electron relaxation occurs as a result of two successive stages, which changes to vibrational relaxation to the ground state. The mechanism and dynamics of electron excitation energy conversion in cytochrome c oxidase are analyzed.
- Добавил в систему: Выгодина Татьяна Владимировна