Role of hydrogen bond alternation and charge transfer states in photoactivation of the Orange Carotenoid Protein

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903671" target="_blank" >RIV/60076658:12310/21:43903671 - isvavai.cz</a>

Result on the web

<a href="https://www.nature.com/articles/s42003-021-02022-3" target="_blank" >https://www.nature.com/articles/s42003-021-02022-3</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s42003-021-02022-3" target="_blank" >10.1038/s42003-021-02022-3</a>

Result language

angličtina

Original language name

Role of hydrogen bond alternation and charge transfer states in photoactivation of the Orange Carotenoid Protein

Original language description

Yaroshevich et al. present a chemical reaction mechanism of a 35-kDa blue light-triggered photoreceptor, the Orange Carotenoid Protein (OCP). They find that photoactivation critically involves the transient formation of a protonated ketocarotenoid (oxocarbenium cation) state. This study suggests the role of charge-transfer states during OCP photoconversion. Here, we propose a possible photoactivation mechanism of a 35-kDa blue light-triggered photoreceptor, the Orange Carotenoid Protein (OCP), suggesting that the reaction involves the transient formation of a protonated ketocarotenoid (oxocarbenium cation) state. Taking advantage of engineering an OCP variant carrying the Y201W mutation, which shows superior spectroscopic and structural properties, it is shown that the presence of Trp201 augments the impact of one critical H-bond between the ketocarotenoid and the protein. This confers an unprecedented homogeneity of the dark-adapted OCP state and substantially increases the yield of the excited photoproduct S*, which is important for the productive photocycle to proceed. A 1.37 angstrom crystal structure of OCP Y201W combined with femtosecond time-resolved absorption spectroscopy, kinetic analysis, and deconvolution of the spectral intermediates, as well as extensive quantum chemical calculations incorporating the effect of the local electric field, highlighted the role of charge-transfer states during OCP photoconversion.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10610 - Biophysics

Project

<a href="/en/project/GA18-21631S" target="_blank" >GA18-21631S: Ultrafast spectroscopy as a tool for elucidation the structure-function relationship in cyanobacterial carotenoid-binding proteins</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2021

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Communications Biology

ISSN

2399-3642

e-ISSN

—

Volume of the periodical

4

Issue of the periodical within the volume

1

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

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UT code for WoS article

000656215600008

EID of the result in the Scopus database

2-s2.0-85105585439