Intrinsic tryptophan fluorescence quenching by iodine in non-canonical amino acid reveals alteration of the hydrogen bond network in the photoactive orange carotenoid protein

Tsoraev, G.V.; Bukhanko, A.Y.; Mamchur, A.A.; Yaroshevich, I.A.; Sluchanko, N.N.; Tseng, H.; Moldenhauer, M.; Budisa, N.; Friedrich, T.; Maksimov, E.G.

Авторы: Tsoraev Georgy V., Bukhanko Antonina Y., Mamchur Alexandra A., Yaroshevich Igor A., Sluchanko Nikolai N., Tseng Hsueh-Wei, Moldenhauer Marcus, Budisa Nediljko, Friedrich Thomas, Maksimov Eugene G.
Журнал: Biochemical and Biophysical Research Communications
Том: 683
Год издания: 2023
Издательство: Academic Press
Местоположение издательства: United States
Номер статьи: 149119
DOI: 10.1016/j.bbrc.2023.10.051
Аннотация: The Orange Carotenoid Protein (OCP) regulates cyanobacterial photosynthetic activity through photoactivation in intense light. A hydrogen bonding network involving the keto-carotenoid oxygen and Y201 and W288 residues prevents the spontaneous activation of dark-adapted OCP. To investigate the role of the hydrogen bonds in OCP photocycling, we introduced non-canonical amino acids near the keto-carotenoid, particularly iodine at the meta-position of Y201. This modification significantly increased the yield of red OCP photoproducts, albeit with a shorter lifetime. Changes in tryptophan fluorescence during photocycling influenced by the presence of iodine near W288 revealed interactions between Y201 and W288 in the absence of the carotenoid in the C-domain. We propose that upon the relaxation of red states, a ternary complex with the carotenoid is formed. Analysis of spectral signatures and interaction energies indicates that the specific iodo-tyrosine configuration enhances interactions between the carotenoid and W288
Добавил в систему: Максимов Евгений Георгиевич

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Intrinsic tryptophan fluorescence quenching by iodine in non-canonical amino acid reveals alteration of the hydrogen bond network in the photoactive orange carotenoid proteinстатья

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