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Autor
Botnarevskii, Viacheslav S 1 Cherepanov, Dmitry A 1 Friedrich, Thomas 1 Gordeliy, Valentin I 1 Gostev, Fedor E 1 Gostev, Timofey S 1 Gushchin, Ivan 1 Khakhulin, Dmitry 1 Kirpichnikov, Mikhail P 1 Kloz, Miroslav 1 Kovalev, Kirill 1 Maksimov, Eugene G 1 Nadtochenko, Victor A 1 Paschenko, Vladimir Z 1 Poddubnyy, Vladimir V 1 Polívka, Tomáš 1 Remeeva, Alina 1 Rubin, Andrew B 1 Shelaev, Ivan V 1 Slonimskiy, Yury B 1
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Pracoviště
A N Bach Institute of Biochemistry Fe... 1 A N Belozersky Institute of Physical ... 1 Chemistry department M 5 Lomonosov Mo... 1 ELI Beamlines Institute of Physics Pr... 1 European XFEL GmbH Schenefeld Germany 1 Faculty of Biology M 5 Lomonosov Mosc... 1 Institut de Biologie Structurale J P ... 1 Institute of Biological Information P... 1 Institute of Crystallography RWTH Aac... 1 Institute of Physics Faculty of Scien... 1 JuStruct Jülich Center for Structural... 1 M M Shemyakin and Yu A Ovchinnikov In... 1 N N Semenov Federal Research Center f... 1 Research Center for Molecular Mechani... 1 Technische Universität Berlin Institu... 1
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Autor
Botnarevskii, Viacheslav S 1 Cherepanov, Dmitry A 1 Friedrich, Thomas 1 Gordeliy, Valentin I 1 Gostev, Fedor E 1 Gostev, Timofey S 1 Gushchin, Ivan 1 Khakhulin, Dmitry 1 Kirpichnikov, Mikhail P 1 Kloz, Miroslav 1 Kovalev, Kirill 1 Maksimov, Eugene G 1 Nadtochenko, Victor A 1 Paschenko, Vladimir Z 1 Poddubnyy, Vladimir V 1 Polívka, Tomáš 1 Remeeva, Alina 1 Rubin, Andrew B 1 Shelaev, Ivan V 1 Slonimskiy, Yury B 1
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Pracoviště
A N Bach Institute of Biochemistry Fe... 1 A N Belozersky Institute of Physical ... 1 Chemistry department M 5 Lomonosov Mo... 1 ELI Beamlines Institute of Physics Pr... 1 European XFEL GmbH Schenefeld Germany 1 Faculty of Biology M 5 Lomonosov Mosc... 1 Institut de Biologie Structurale J P ... 1 Institute of Biological Information P... 1 Institute of Crystallography RWTH Aac... 1 Institute of Physics Faculty of Scien... 1 JuStruct Jülich Center for Structural... 1 M M Shemyakin and Yu A Ovchinnikov In... 1 N N Semenov Federal Research Center f... 1 Research Center for Molecular Mechani... 1 Technische Universität Berlin Institu... 1
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Nature Open Access od 2018-12-01
PubMed Central od 2018
Europe PubMed Central od 2018
ProQuest Central od 2018-01-01
ROAD: Directory of Open Access Scholarly Resources od 2018
PubMed
33972665
DOI
10.1038/s42003-021-02022-3
Knihovny.cz E-zdroje
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.
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