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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

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
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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
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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. 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
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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
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Article ; Online: State of the phycobilisome determines effective absorption cross-section of Photosystem II in Synechocystis sp. PCC 6803.

Protasova, Elena A / Antal, Taras K / Zlenko, Dmitry V / Elanskaya, Irina V / Lukashev, Evgeny P / Friedrich, Thomas / Mironov, Kirill S / Sluchanko, Nikolai N / Ge, Baosheng / Qin, Song / Maksimov, Eugene G

Biochimica et biophysica acta. Bioenergetics

2021 Volume 1862, Issue 12, Page(s) 148494

Abstract: Quenching of excess excitation energy is necessary for the photoprotection of light-harvesting complexes. In cyanobacteria, quenching of phycobilisome (PBS) excitation energy is induced by the Orange Carotenoid Protein (OCP), which becomes photoactivated ...

Abstract	Quenching of excess excitation energy is necessary for the photoprotection of light-harvesting complexes. In cyanobacteria, quenching of phycobilisome (PBS) excitation energy is induced by the Orange Carotenoid Protein (OCP), which becomes photoactivated under high light conditions. A decrease in energy transfer efficiency from the PBSs to the reaction centers decreases photosystem II (PS II) activity. However, quantitative analysis of OCP-induced photoprotection in vivo is complicated by similar effects of both photochemical and non-photochemical quenching on the quantum yield of the PBS fluorescence overlapping with the emission of chlorophyll. In the present study, we have analyzed chlorophyll a fluorescence induction to estimate the effective cross-section of PS II and compared the effects of reversible OCP-dependent quenching of PBS fluorescence with reduction of PBS content upon nitrogen starvation or mutations of key PBS components. This approach allowed us to estimate the dependency of the rate constant of PS II primary electron acceptor reduction on the amount of PBSs in the cell. We found that OCP-dependent quenching triggered by blue light affects approximately half of PBSs coupled to PS II, indicating that under normal conditions, the concentration of OCP is not sufficient for quenching of all PBSs coupled to PS II.
MeSH term(s)	Photosystem II Protein Complex ; Phycobilisomes
Chemical Substances	Photosystem II Protein Complex ; Phycobilisomes
Language	English
Publishing date	2021-09-15
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.2021.148494
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Article: State of the phycobilisome determines effective absorption cross-section of Photosystem II in Synechocystis sp. PCC 6803

Protasova, Elena A. / Antal, Taras K. / Zlenko, Dmitry V. / Elanskaya, Irina V. / Lukashev, Evgeny P. / Friedrich, Thomas / Mironov, Kirill S. / Sluchanko, Nikolai N. / Ge, Baosheng / Qin, Song / Maksimov, Eugene G.

Biochimica et biophysica acta. 2021 Dec. 01, v. 1862, no. 12

2021

Abstract	Quenching of excess excitation energy is necessary for the photoprotection of light-harvesting complexes. In cyanobacteria, quenching of phycobilisome (PBS) excitation energy is induced by the Orange Carotenoid Protein (OCP), which becomes photoactivated under high light conditions. A decrease in energy transfer efficiency from the PBSs to the reaction centers decreases photosystem II (PS II) activity. However, quantitative analysis of OCP-induced photoprotection in vivo is complicated by similar effects of both photochemical and non-photochemical quenching on the quantum yield of the PBS fluorescence overlapping with the emission of chlorophyll. In the present study, we have analyzed chlorophyll a fluorescence induction to estimate the effective cross-section of PS II and compared the effects of reversible OCP-dependent quenching of PBS fluorescence with reduction of PBS content upon nitrogen starvation or mutations of key PBS components. This approach allowed us to estimate the dependency of the rate constant of PS II primary electron acceptor reduction on the amount of PBSs in the cell. We found that OCP-dependent quenching triggered by blue light affects approximately half of PBSs coupled to PS II, indicating that under normal conditions, the concentration of OCP is not sufficient for quenching of all PBSs coupled to PS II.
Keywords	absorption ; blue light ; carotenoids ; chlorophyll ; energy transfer ; fluorescence ; nitrogen ; photochemistry ; phycobilisome ; quantitative analysis ; radiation resistance ; starvation
Language	English
Dates of publication	2021-1201
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282711-6
ISSN	0005-2728 ; 0304-4173
ISSN	0005-2728 ; 0304-4173
DOI	10.1016/j.bbabio.2021.148494
Database	NAL-Catalogue (AGRICOLA)

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Article: Phycobilisomes from the mutant cyanobacterium Synechocystis sp. PCC 6803 missing chromophore domain of ApcE.

Elanskaya, Irina V / Zlenko, Dmitry V / Lukashev, Evgeny P / Suzina, Natalia E / Kononova, Irena A / Stadnichuk, Igor N

Biochimica et biophysica acta. Bioenergetics

2018 Volume 1859, Issue 4, Page(s) 280–291

Abstract: Phycobilisome (PBS) is a giant photosynthetic antenna associated with the thylakoid membranes of cyanobacteria and red algae. PBS consists of two domains: central core and peripheral rods assembled of disc-shaped phycobiliprotein aggregates and linker ... ...

Abstract	Phycobilisome (PBS) is a giant photosynthetic antenna associated with the thylakoid membranes of cyanobacteria and red algae. PBS consists of two domains: central core and peripheral rods assembled of disc-shaped phycobiliprotein aggregates and linker polypeptides. The study of the PBS architecture is hindered due to the lack of the data on the structure of the large ApcE-linker also called L
MeSH term(s)	Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Energy Transfer ; Gene Expression ; Genetic Engineering ; Light ; Mutation ; Photosystem I Protein Complex/chemistry ; Photosystem I Protein Complex/genetics ; Photosystem I Protein Complex/metabolism ; Photosystem II Protein Complex/chemistry ; Photosystem II Protein Complex/genetics ; Photosystem II Protein Complex/metabolism ; Phycobilisomes/genetics ; Phycobilisomes/metabolism ; Phycobilisomes/radiation effects ; Phycobilisomes/ultrastructure ; Protein Binding ; Protein Domains ; Sequence Deletion ; Synechocystis/genetics ; Synechocystis/metabolism ; Synechocystis/radiation effects ; Synechocystis/ultrastructure ; Thylakoids/metabolism ; Thylakoids/radiation effects ; Thylakoids/ultrastructure
Chemical Substances	Bacterial Proteins ; Photosystem I Protein Complex ; Photosystem II Protein Complex ; Phycobilisomes ; orange carotenoid protein, Synechocystis
Language	English
Publishing date	2018-01-31
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0005-2728 ; 0006-3002 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0005-2728 ; 0006-3002 ; 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.2018.01.003
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Article: Fluorescence changes accompanying short-term light adaptations in photosystem I and photosystem II of the cyanobacterium Synechocystis sp. PCC 6803 and phycobiliprotein-impaired mutants: State 1/State 2 transitions and carotenoid-induced quenching of phycobilisomes.

Stadnichuk, Igor N / Lukashev, Evgeny P / Elanskaya, Irina V

Photosynthesis research

2009 Volume 99, Issue 3, Page(s) 227–241

Abstract: The features of the two types of short-term light-adaptations of photosynthetic apparatus, State 1/State 2 transitions, and non-photochemical fluorescence quenching of phycobilisomes (PBS) by orange carotene-protein (OCP) were compared in the ... ...

Abstract	The features of the two types of short-term light-adaptations of photosynthetic apparatus, State 1/State 2 transitions, and non-photochemical fluorescence quenching of phycobilisomes (PBS) by orange carotene-protein (OCP) were compared in the cyanobacterium Synechocystis sp. PCC 6803 wild type, CK pigment mutant lacking phycocyanin, and PAL mutant totally devoid of phycobiliproteins. The permanent presence of PBS-specific peaks in the in situ action spectra of photosystem I (PSI) and photosystem II (PSII), as well as in the 77 K fluorescence excitation spectra for chlorophyll emission at 690 nm (PSII) and 725 nm (PSI) showed that PBS are constitutive antenna complexes of both photosystems. The mutant strains compensated the lack of phycobiliproteins by higher PSII content and by intensification of photosynthetic linear electron transfer. The detectable changes of energy migration from PBS to the PSI and PSII in the Synechocystis wild type and the CK mutant in State 1 and State 2 according to the fluorescence excitation spectra measurements were not registered. The constant level of fluorescence emission of PSI during State 1/State 2 transitions and simultaneous increase of chlorophyll fluorescence emission of PSII in State 1 in Synechocystis PAL mutant allowed to propose that spillover is an unlikely mechanism of state transitions. Blue-green light absorbed by OCP diminished the rout of energy from PBS to PSI while energy migration from PBS to PSII was less influenced. Therefore, the main role of OCP-induced quenching of PBS is the limitation of PSI activity and cyclic electron transport under relatively high light conditions.
MeSH term(s)	Adaptation, Physiological/radiation effects ; Carotenoids/physiology ; Electron Transport/physiology ; Gene Expression Regulation, Bacterial/genetics ; Light ; Mutation ; Photosystem I Protein Complex/physiology ; Photosystem I Protein Complex/radiation effects ; Photosystem II Protein Complex/physiology ; Photosystem II Protein Complex/radiation effects ; Phycobiliproteins/genetics ; Phycobiliproteins/metabolism ; Spectrometry, Fluorescence ; Synechocystis/genetics ; Synechocystis/physiology
Chemical Substances	Photosystem I Protein Complex ; Photosystem II Protein Complex ; Phycobiliproteins ; Carotenoids (36-88-4)
Language	English
Publishing date	2009-01-24
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1475688-2
ISSN	1573-5079 ; 0166-8595
ISSN (online)	1573-5079
ISSN	0166-8595
DOI	10.1007/s11120-009-9402-x
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Article ; Online: Synechocystis sp. PCC 6803 mutant lacking both photosystems exhibits strong carotenoid-induced quenching of phycobilisome fluorescence.

Rakhimberdieva, Marina G / Kuzminov, Fedor I / Elanskaya, Irina V / Karapetyan, Navassard V

FEBS letters

2011 Volume 585, Issue 3, Page(s) 585–589

Abstract: Blue light induced quenching in a Synechocystis sp. PCC 6803 strain lacking both photosystems is only related to allophycocyanin fluorescence. A fivefold decrease in the fluorescence level in two bands near 660 and 680 nm is attributed to different ... ...

Abstract	Blue light induced quenching in a Synechocystis sp. PCC 6803 strain lacking both photosystems is only related to allophycocyanin fluorescence. A fivefold decrease in the fluorescence level in two bands near 660 and 680 nm is attributed to different allophycocyanin forms in the phycobilisome core. Some low-heat sensitive component inactivated at 53°C is involved in the quenching process. Enormous allophycocyanin fluorescence in the absence of the photosystems reveals a dark stage in this quenching. Thus, we present evidence that light activation of the carotenoid-binding protein and formation of a quenching center within the phycobilisome core in vivo are discrete events in a multistep process.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Proteins/radiation effects ; Carotenoids/chemistry ; Carotenoids/metabolism ; Fluorescence ; Hot Temperature ; Kinetics ; Light ; Mutation ; Photosystem I Protein Complex/genetics ; Photosystem II Protein Complex/genetics ; Phycobilisomes/chemistry ; Phycobilisomes/metabolism ; Phycobilisomes/radiation effects ; Spectrometry, Fluorescence ; Synechocystis/genetics ; Synechocystis/metabolism ; Synechocystis/radiation effects
Chemical Substances	Bacterial Proteins ; Photosystem I Protein Complex ; Photosystem II Protein Complex ; Phycobilisomes ; Carotenoids (36-88-4)
Language	English
Publishing date	2011-02-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2011.01.013
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Article ; Online: Role of the PB-loop in ApcE and phycobilisome core function in cyanobacterium Synechocystis sp. PCC 6803.

Zlenko, Dmitry V / Elanskaya, Irina V / Lukashev, Evgeny P / Bolychevtseva, Yulia V / Suzina, Natalia E / Pojidaeva, Elena S / Kononova, Irena A / Loktyushkin, Aleksey V / Stadnichuk, Igor N

Biochimica et biophysica acta. Bioenergetics

2018 Volume 1860, Issue 2, Page(s) 155–166

Abstract: The phycobilisome (PBS) is a giant highly-structured pigment-protein antenna of cyanobacteria and red algae. PBS is composed of the phycobiliproteins and several linker polypeptides. The large core-membrane linker protein ( ... ...

Abstract	The phycobilisome (PBS) is a giant highly-structured pigment-protein antenna of cyanobacteria and red algae. PBS is composed of the phycobiliproteins and several linker polypeptides. The large core-membrane linker protein (L
MeSH term(s)	Bacterial Proteins/physiology ; Cyanobacteria ; Energy Transfer ; Mutation ; Photosystem II Protein Complex/metabolism ; Phycobiliproteins/physiology ; Phycobilisomes/genetics ; Rhodophyta ; Sequence Deletion ; Synechocystis/chemistry ; Thylakoids/metabolism
Chemical Substances	Bacterial Proteins ; Photosystem II Protein Complex ; Phycobiliproteins ; Phycobilisomes
Language	English
Publishing date	2018-11-07
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.2018.10.004
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