Probing of carotenoid-tryptophan hydrogen bonding dynamics in the single-tryptophan photoactive Orange Carotenoid Protein.

Scientific Reports
Eugene G MaksimovThomas Friedrich

Abstract

The photoactive Orange Carotenoid Protein (OCP) plays a key role in cyanobacterial photoprotection. In OCP, a single non-covalently bound keto-carotenoid molecule acts as a light intensity sensor, while the protein is responsible for forming molecular contacts with the light-harvesting antenna, the fluorescence of which is quenched by OCP. Activation of this physiological interaction requires signal transduction from the photoexcited carotenoid to the protein matrix. Recent works revealed an asynchrony between conformational transitions of the carotenoid and the protein. Intrinsic tryptophan (Trp) fluorescence has provided valuable information about the protein part of OCP during its photocycle. However, wild-type OCP contains five Trp residues, which makes extraction of site-specific information impossible. In this work, we overcame this problem by characterizing the photocycle of a fully photoactive OCP variant (OCP-3FH) with only the most critical tryptophan residue (Trp-288) in place. Trp-288 is of special interest because it forms a hydrogen bond to the carotenoid's keto-oxygen to keep OCP in its dark-adapted state. Using femtosecond pump-probe fluorescence spectroscopy we analyzed the photocycle of OCP-3FH and determined ...Continue Reading

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Citations

May 12, 2021·Communications Biology·Igor A YaroshevichMikhail P Kirpichnikov
Jul 13, 2021·The Journal of Physical Chemistry Letters·Mattia BondanzaBenedetta Mennucci
Dec 18, 2020·Journal of the American Chemical Society·Mattia BondanzaBenedetta Mennucci

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Methods Mentioned

BETA
X-ray
Fluorescence
size-exclusion chromatography
size-exclusion spectrochromatography
FRET

Software Mentioned

SPCImage
SPCM
Origin Pro
OriginLab

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