The photocycle of orange carotenoid protein conceals distinct intermediates and asynchronous changes in the carotenoid andprotein components

Maksimov, E.G.; Sluchanko, N.N.; Slonimskiy, Y.B.; Slutskaya, E.A.; Stepanov, A.V.; Argentova-Stevens, A.M.; Shirshin, E.A.; Tsoraev, G.V.; Klementiev, K.E.; Slatinskaya, O.V.; Lukashev, E.P.; Friedrich, T.; Paschenko, V.Z.; Rubin, A.B.

Статья опубликована в высокорейтинговом журнале

Информация о цитировании статьи получена из Web of Science, Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 19 декабря 2017 г.

Авторы: Maksimov E.G., Sluchanko N.N., Slonimskiy Y.B., Slutskaya E.A., Stepanov A.V., Argentova-Stevens A.M., Shirshin E.A., Tsoraev G.V., Klementiev K.E., Slatinskaya O.V., Lukashev E.P., Friedrich T., Paschenko V.Z., Rubin A.B.
Журнал: Scientific reports
Номер: 7
Год издания: 2017
Издательство: Nature Publishing Group
Местоположение издательства: United Kingdom
Первая страница: 15548
DOI: 10.1038/s41598-017-15520-4
Аннотация: The 35-kDa Orange Carotenoid Protein (OCP) is responsible for photoprotection in cyanobacteria. It acts as a light intensity sensor and efficient quencher of phycobilisome excitation. Photoactivation triggers large-scale conformational rearrangements to convert OCP from the orange OCPO state to the red active signaling state, OCPR, as demonstrated by various structural methods. Such rearrangements imply a complete, yet reversible separation of structural domains and translocation of the carotenoid. Recently, dynamic crystallography of OCPO suggested the existence of photocycle intermediates with small-scale rearrangements that may trigger further transitions. In this study, we took advantage of single 7 ns laser pulses to study carotenoid absorption transients in OCP on the time-scale from 100 ns to 10 s, which allowed us to detect a red intermediate state preceding the red signaling state, OCPR. In addition, time-resolved fluorescence spectroscopy and the assignment of carotenoid-induced quenching of different tryptophan residues derived thereof revealed a novel orange intermediate state, which appears during the relaxation of photoactivated OCPR to OCPO. Our results show asynchronous changes between the carotenoid- and protein-associated kinetic components in a refined mechanistic model of the OCP photocycle, but also introduce new kinetic signatures for future studies of OCP photoactivity and photoprotection.
Добавил в систему: Максимов Евгений Георгиевич

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The photocycle of orange carotenoid protein conceals distinct intermediates and asynchronous changes in the carotenoid andprotein componentsстатья

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