Evidence map›Paper›PMID 33972665›Full record

ArticleCommunications biology2021

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

Igor A Yaroshevich, Eugene G Maksimov, Nikolai N Sluchanko, Dmitry V Zlenko, Alexey V Stepanov, Ekaterina A Slutskaya, Yury B Slonimskiy, Viacheslav S Botnarevskii, Alina Remeeva, Ivan Gushchin and 15 more

Abstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

  1. Atomistic simulations reveal the photoactivation mechanism of a carotenoid-binding photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

25 authors.

Igor A YaroshevichFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.ORCID 0000-0002-8525-5568
Eugene G MaksimovFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia. emaksimoff@yandex.ru.ORCID 0000-0001-6767-1501
Nikolai N SluchankoA.N. Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, Moscow, Russia.ORCID 0000-0002-8608-1416
Dmitry V ZlenkoFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Alexey V StepanovM.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.ORCID 0000-0003-1616-4408
Ekaterina A SlutskayaFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Yury B SlonimskiyFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Viacheslav S BotnarevskiiFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Alina RemeevaResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Ivan GushchinResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.ORCID 0000-0002-5348-6070
Kirill KovalevResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Valentin I GordeliyResearch Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.ORCID 0000-0001-5782-5896
Ivan V ShelaevN.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, Moscow, Russia.
Fedor E GostevN.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, Moscow, Russia.
Dmitry KhakhulinEuropean XFEL GmbH, Schenefeld, Germany.
Vladimir V PoddubnyyChemistry department, M.V. Lomonosov Moscow State University, Moscow, Russia.
Timofey S GostevFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Dmitry A CherepanovN.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, Moscow, Russia.
Tomáš PolívkaInstitute of Physics, Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic.
Miroslav KlozELI-Beamlines, Institute of Physics, Praha, Czech Republic.
Thomas FriedrichTechnische Universität Berlin, Institute of Chemistry PC14, Berlin, Germany.ORCID 0000-0003-2835-2895
Vladimir Z PaschenkoFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Victor A NadtochenkoN.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, Moscow, Russia.
Andrew B RubinFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.
Mikhail P KirpichnikovFaculty of Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 Å 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.

Indexed as

PhotochemistryBacterial ProteinsCarotenoidsCrystallographyHydrogen BondingKineticsModels, MolecularProtein ConformationBacterial ProteinsCarotenoidsorange carotenoid protein, Synechocystis

Identifiers

PMID33972665
PMCPMC8110590

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.