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  1. Article ; Online: Roles of ApcD and orange carotenoid protein in photoinduction of electron transport upon dark-light transition in the Synechocystis PCC 6803 mutant deficient in flavodiiron protein Flv1.

    Elanskaya, Irina V / Bulychev, Alexander A / Lukashev, Evgeny P / Muronets, Elena M / Maksimov, Eugene G

    Photosynthesis research

    2023  Volume 159, Issue 2-3, Page(s) 97–114

    Abstract: Flavodiiron proteins Flv1/Flv3 accept electrons from photosystem (PS) I. In this work we investigated light adaptation mechanisms of Flv1-deficient mutant of Synechocystis PCC 6803, incapable to form the Flv1/Flv3 heterodimer. First seconds of dark-light ...

    Abstract Flavodiiron proteins Flv1/Flv3 accept electrons from photosystem (PS) I. In this work we investigated light adaptation mechanisms of Flv1-deficient mutant of Synechocystis PCC 6803, incapable to form the Flv1/Flv3 heterodimer. First seconds of dark-light transition were studied by parallel measurements of light-induced changes in chlorophyll fluorescence, P700 redox transformations, fluorescence emission at 77 K, and OCP-dependent fluorescence quenching. During the period of Calvin cycle activation upon dark-light transition, the linear electron transport (LET) in wild type is supported by the Flv1/Flv3 heterodimer, whereas in Δflv1 mutant activation of LET upon illumination is preceded by cyclic electron flow that maintains State 2. The State 2-State 1 transition and Orange Carotenoid Protein (OCP)-dependent non-photochemical quenching occur independently of each other, begin in about 10 s after the illumination of the cells and are accompanied by a short-term re-reduction of the PSI reaction center (P700
    MeSH term(s) Electron Transport ; Synechocystis/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Mutation ; Oxidation-Reduction ; Photosystem I Protein Complex/genetics ; Photosystem I Protein Complex/metabolism ; Carotenoids/metabolism ; Chlorophyll/metabolism ; Photosystem II Protein Complex/genetics ; Photosystem II Protein Complex/metabolism
    Chemical Substances Bacterial Proteins ; Photosystem I Protein Complex ; Carotenoids (36-88-4) ; Chlorophyll (1406-65-1) ; Photosystem II Protein Complex
    Language English
    Publishing date 2023-04-24
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1475688-2
    ISSN 1573-5079 ; 0166-8595
    ISSN (online) 1573-5079
    ISSN 0166-8595
    DOI 10.1007/s11120-023-01019-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Deficiency in flavodiiron protein Flv3 promotes cyclic electron flow and state transition under high light in the cyanobacterium Synechocystis sp. PCC 6803

    Elanskaya, Irina V / Bulychev, Alexander A / Lukashev, Evgeny P / Muronets, Elena M

    Biochimica et biophysica acta. 2021 Jan. 01, v. 1862, no. 1

    2021  

    Abstract: Photosynthetic organisms adjust their activity to changes in irradiance by different ways, including the operation of cyclic electron flow around photosystem I (PSI) and state transitions that redistribute amounts of light energy absorbed by PSI and PSII. ...

    Abstract Photosynthetic organisms adjust their activity to changes in irradiance by different ways, including the operation of cyclic electron flow around photosystem I (PSI) and state transitions that redistribute amounts of light energy absorbed by PSI and PSII. In dark-acclimated wild type cells of Synechocystis PCC 6803, linear electron transport was activated after the first 500 ms of illumination, while cyclic electron flow around PSI was long predominant in the mutant deficient in flavodiiron protein Flv3. Chlorophyll P700 oxidation associated with activation of linear electron flow extended in the Flv3⁻ mutant to several tens of seconds and included a P700⁺ re-reduction phase. Parallel monitoring of chlorophyll fluorescence and the redox state of P700 indicated that, at low light intensity both in wild type and in the Flv3⁻ mutant, the transient re-reduction step coincided in time with S-M fluorescence rise, which reflected state 2–state 1 transition (Kaňa et al., 2012). Despite variations in the initial redox state of plastoquinone pool, the oxidases-deficient mutant, succinate dehydrogenase-deficient mutant, and wild type cells did not show the S-M rise under high-intensity light until additional Flv3⁻ mutation was introduced in these strains. Thus, the lack of available electron acceptor for PSI was the main cause for the appearance of S-M fluorescence rise under high light. It is concluded that the lack of Flv3 protein promotes cyclic electron flow around PSI and facilitates the subsequent state 2–state 1 transition in the absence of strict relation to the dark-operated pathways of plastoquinone reduction or oxidation.
    Keywords Synechocystis sp. PCC 6803 ; appearance (quality) ; autotrophs ; cells ; chlorophyll ; electron transfer ; energy ; flow ; fluorescence ; light intensity ; lighting ; monitoring ; mutants ; mutation ; oxidation ; photosystem I ; photosystem II ; plastoquinones ; strains ; succinic acid
    Language English
    Dates of publication 2021-0101
    Publishing place Elsevier B.V.
    Document type Article
    Note NAL-light
    ZDB-ID 282711-6
    ISSN 0005-2728 ; 0304-4173
    ISSN 0005-2728 ; 0304-4173
    DOI 10.1016/j.bbabio.2020.148318
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

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  3. Article ; Online: Deficiency in flavodiiron protein Flv3 promotes cyclic electron flow and state transition under high light in the cyanobacterium Synechocystis sp. PCC 6803.

    Elanskaya, Irina V / Bulychev, Alexander A / Lukashev, Evgeny P / Muronets, Elena M

    Biochimica et biophysica acta. Bioenergetics

    2020  Volume 1862, Issue 1, Page(s) 148318

    Abstract: Photosynthetic organisms adjust their activity to changes in irradiance by different ways, including the operation of cyclic electron flow around photosystem I (PSI) and state transitions that redistribute amounts of light energy absorbed by PSI and PSII. ...

    Abstract Photosynthetic organisms adjust their activity to changes in irradiance by different ways, including the operation of cyclic electron flow around photosystem I (PSI) and state transitions that redistribute amounts of light energy absorbed by PSI and PSII. In dark-acclimated wild type cells of Synechocystis PCC 6803, linear electron transport was activated after the first 500 ms of illumination, while cyclic electron flow around PSI was long predominant in the mutant deficient in flavodiiron protein Flv3. Chlorophyll P700 oxidation associated with activation of linear electron flow extended in the Flv3
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Electron Transport/genetics ; Electron Transport/radiation effects ; Light ; Mutation ; Photosystem I Protein Complex/genetics ; Photosystem I Protein Complex/metabolism ; Photosystem II Protein Complex/genetics ; Photosystem II Protein Complex/metabolism ; Synechocystis/genetics ; Synechocystis/metabolism
    Chemical Substances Bacterial Proteins ; Photosystem I Protein Complex ; Photosystem II Protein Complex
    Language English
    Publishing date 2020-09-24
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbabio.2020.148318
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Photoinduction of electron transport on the acceptor side of PSI in Synechocystis PCC 6803 mutant deficient in flavodiiron proteins Flv1 and Flv3.

    Bulychev, Alexander A / Cherkashin, Alexander A / Muronets, Elena M / Elanskaya, Irina V

    Biochimica et biophysica acta. Bioenergetics

    2018  Volume 1859, Issue 10, Page(s) 1086–1095

    Abstract: After transferring the dark-acclimated cyanobacteria to light, flavodiiron proteins Flv1/Flv3 serve as a main electron acceptor for PSI within the first seconds because Calvin cycle enzymes are inactive in the dark. Synechocystis PCC 6803 mutant Δflv1/ ... ...

    Abstract After transferring the dark-acclimated cyanobacteria to light, flavodiiron proteins Flv1/Flv3 serve as a main electron acceptor for PSI within the first seconds because Calvin cycle enzymes are inactive in the dark. Synechocystis PCC 6803 mutant Δflv1/Δflv3 devoid of Flv1 and Flv3 retained the PSI chlorophyll P700 in the reduced state over 10 s (Helman et al., 2003; Allahverdiyeva et al., 2013). Study of P700 oxidoreduction transients in dark-acclimated Δflv1/Δflv3 mutant under the action of successive white light pulses separated by dark intervals of various durations indicated that the delayed oxidation of P700 was determined by light activation of electron transport on the acceptor side of PSI. We show that the light-induced redox transients of chlorophyll P700 in dark-acclimated Δflv1/Δflv3 proceed within 2 min, as opposed to 1-3 s in the wild type, and comprise a series of kinetic stages. The release of rate-limiting steps was eliminated by iodoacetamide, an inhibitor of Calvin cycle enzymes. Conversely, the creation with methyl viologen of a bypass electron flow to O
    Language English
    Publishing date 2018-06-19
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbabio.2018.06.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
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