Light- and pH-dependent structural changes in cyanobacteriochrome AnPixJg2.

Autor: Altmayer S; Institut Für Analytische Chemie, Universität Leipzig, Linnéstraße 3, 04103, Leipzig, Germany., Köhler L; Institut Für Analytische Chemie, Universität Leipzig, Linnéstraße 3, 04103, Leipzig, Germany., Bielytskyi P; Institut Für Analytische Chemie, Universität Leipzig, Linnéstraße 3, 04103, Leipzig, Germany., Gärtner W; Institut Für Analytische Chemie, Universität Leipzig, Linnéstraße 3, 04103, Leipzig, Germany., Matysik J; Institut Für Analytische Chemie, Universität Leipzig, Linnéstraße 3, 04103, Leipzig, Germany., Wiebeler C; Institut Für Analytische Chemie, Universität Leipzig, Linnéstraße 3, 04103, Leipzig, Germany. christian.wiebeler@uni-leipzig.de.; Leibniz-Institut Für Oberflächenmodifizierung, Permoserstraße 15, 04318, Leipzig, Germany. christian.wiebeler@uni-leipzig.de., Song C; Institut Für Analytische Chemie, Universität Leipzig, Linnéstraße 3, 04103, Leipzig, Germany. chen.song@uni-leipzig.de.
Jazyk: angličtina
Zdroj: Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology [Photochem Photobiol Sci] 2022 Apr; Vol. 21 (4), pp. 447-469. Date of Electronic Publication: 2022 Apr 08.
DOI: 10.1007/s43630-022-00204-4
Abstrakt: Cyanobacteriochromes (CBCRs) are phytochrome-related photosensory proteins that play an essential role in regulating phototaxis, chromatic acclimation, and cell aggregation in cyanobacteria. Here, we apply solid-state NMR spectroscopy to the red/green GAF2 domain of the CBCR AnPixJ assembled in vitro with a uniformly 13 C- and 15 N-labeled bilin chromophore, tracking changes in electronic structure, geometry, and structural heterogeneity of the chromophore as well as intimate contacts between the chromophore and protein residues in the photocycle. Our data confirm that the bilin ring D is strongly twisted with respect to the B-C plane in both dark and photoproduct states. We also identify a greater structural heterogeneity of the bilin chromophore in the photoproduct than in the dark state. In addition, the binding pocket is more hydrated in the photoproduct. Observation of interfacial 1 H contacts of the photoproduct chromophore, together with quantum mechanics/molecular mechanics (QM/MM)-based structural models for this photoproduct, clearly suggests the presence of a biprotonated (cationic) imidazolium side-chain for a conserved histidine residue (322) at a distance of ~2.7 Å, generalizing the recent theoretical findings that explicitly link the structural heterogeneity of the dark-state chromophore to the protonation of this specific residue. Moreover, we examine pH effects on this in vitro assembled holoprotein, showing a substantially altered electronic structure and protonation of the photoproduct chromophore even with a small pH drop from 7.8 to 7.2. Our studies provide further information regarding the light- and pH-induced changes of the chromophore and the rearrangements of the hydrogen-bonding and electrostatic interaction network around it. Possible correlations between structural heterogeneity of the chromophore, protonation of the histidine residue nearby, and hydration of the pocket in both photostates are discussed.
(© 2022. The Author(s).)
Databáze: MEDLINE
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