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Individual heme a and heme a3 contributions to the Soret absorption spectrum of the reduced bovine cytochrome c oxidaseстатья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Diuba* Artem V., Vygodina Tatiana V., Azarkina Natalia V., Arutyunyan Alexander M., Soulimane Tewfik, Vos Marten H., Konstantinov Alexander A.
- Журнал: Biochimica et Biophysica Acta - Bioenergetics
- Том: 1863
- Номер: 10
- Год издания: 2022
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Номер статьи: 148937
- DOI: 10.1016/j.bbabio.2022.148937
- Аннотация: Bovine cytochrome c oxidase (CcO) contains two hemes, a and a3, chemically identical but differing in coordination and spin state. The Soret absorption band of reduced aa3-typecytochrome c oxidase consists of overlapping bands of the hemes a2+ and a32+. It shows a peak at ~444 nm and a distinct shoulder at ~425 nm. However, attribution of individual spectral lineshapes to hemes a2+ and a32+ in the Soret is controversial. In the present work, we characterized spectral contributions of hemes a2+ and a32+using two approaches. First, we reconstructed bovine CcOheme a2+ spectrum using a selective Ca2+-induced spectral shift of the heme a2+. Second, we investigated photobleaching of the reduced Thermus thermophilusba3- and bovine aa3-oxidases in the Soret induced by femtosecond laser pulses in the Q-band. The resolved spectra show splitting of the electronic B0x-, B0y-transitions of both reduced hemes. The heme a2+ spectrum is shifted to the red relative to heme a32+ spectrum. The ~425 nm shoulder is mostly attributed to heme a32+.
- Добавил в систему: Выгодина Татьяна Владимировна