Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix

0537885 - FZÚ 2021 RIV NL eng J - Journal Article
Kuznetsova, V. - Dominguez-Martin, M.A. - Bao, H. - Gupta, S. - Sutter, M. - Kloz, Miroslav - Rebarz, Mateusz - Přeček, Martin - Chen, Y. - Petzold, Ch.J. - Ralston, C. Y. - Kerfeld, C.A. - Polívka, T.
Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix.
Biochimica Et Biophysica Acta-Bioenergetics. Roč. 1861, č. 2 (2020), s. 1-41, č. článku 148120. ISSN 0005-2728. E-ISSN 1879-2650
Research Infrastructure: ELI Beamlines III - 90141
Institutional support: RVO:68378271
Keywords : OCP1 * OCP2 * photoactivation * X-ray footprinting * ulltrafast spectroscopy
OECD category: Physical chemistry
Impact factor: 3.991, year: 2020
Method of publishing: Limited access
https://doi.org/10.1016/j.bbabio.2019.148120

The orange carotenoid protein (OCP) is a structurally and functionally modular photoactive protein involved in cyanobacterial photoprotection. Recently, based on bioinformatic analysis and phylogenetic relationships, new families of OCP have been described, OCP2 and OCPx. The first characterization of the OCP2 showed both faster photoconversion and back-conversion, and lower fluorescence quenching of phycobilisomes relative to the well-characterized OCP1. Moreover, OCP2 is not regulated by the fluorescence recovery protein (FRP). In this work, we present a comprehensive study combining ultrafast spectroscopy and structural analysis to compare the photoactivation mechanisms of OCP1 and OCP2 from Tolypothrix PCC 7601. We show that despite significant differences in their functional characteristics, the spectroscopic properties of OCP1 and OCP2 are comparable. This indicates that the OCP functionality is not directly related to the spectroscopic properties of the bound carotenoid.
Permanent Link: http://hdl.handle.net/11104/0315723