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Relationship between the structure and physicochemical properties of cytochrome c546/556 from the bacterium Thioalkalivibrio paradoxus ARh1статья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 23 января 2026 г.
- Авторы: Varfolomeeva L.A., Solovieva A.Y., Shipkov N.S., Sluchanko N.N., Boyko K.M., Khrenova M.G., Tikhonova T.V., Popov V.O.
- Журнал: Biochemical and Biophysical Research Communications
- Том: 778
- Год издания: 2025
- Издательство: Academic Press
- Местоположение издательства: United States
- Номер статьи: 152340
- DOI: 10.1016/j.bbrc.2025.152340
- Аннотация: An interplay between the structural and physicochemical properties of the monoheme cytochromes of type c hasbeen extensively studied. However new proteins belonging to this diverse family continue to reveal some noveland unique features. Here, we present the 1.15 Å structure of the low-potential cytochrome c546/556 from thebacterium Thioalkalivibrio paradoxus ARh1, which exhibits the prominent splitting of the Q bands in UV–visiblespectra even at room temperature. The data obtained suggest that two conformations of the propionate 7 of theheme are responsible for the splitting of the Q bands. We propose that the degree of the splitting of the Q bands iscorrelated with the conformational lability of the heme propionates.
- Добавил в систему: Киселевский Дмитрий Борисович
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