LIVIVO - Search results -

Search results

Result 1 - 10 of total 16

Search options

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
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- Full text online
- Order with fees

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)

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

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
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Engineering the photoactive orange carotenoid protein with redox-controllable structural dynamics and photoprotective function.

Slonimskiy, Yury B / Maksimov, Eugene G / Lukashev, Evgeny P / Moldenhauer, Marcus / Friedrich, Thomas / Sluchanko, Nikolai N

Biochimica et biophysica acta. Bioenergetics

2020 Volume 1861, Issue 5-6, Page(s) 148174

Abstract: Photosynthesis requires various photoprotective mechanisms for survival of organisms in high light. In cyanobacteria exposed to high light, the Orange Carotenoid Protein (OCP) is reversibly photoswitched from the orange ( ... ...

Abstract	Photosynthesis requires various photoprotective mechanisms for survival of organisms in high light. In cyanobacteria exposed to high light, the Orange Carotenoid Protein (OCP) is reversibly photoswitched from the orange (OCP
MeSH term(s)	Adaptation, Physiological ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Disulfides/chemistry ; Fluorescence ; Light ; Models, Molecular ; Oxidation-Reduction/radiation effects ; Phycobilisomes/metabolism ; Protein Engineering
Chemical Substances	Bacterial Proteins ; Disulfides ; Phycobilisomes ; orange carotenoid protein, Synechocystis
Language	English
Publishing date	2020-02-12
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.2020.148174
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Engineering the photoactive orange carotenoid protein with redox-controllable structural dynamics and photoprotective function

Slonimskiy, Yury B / Friedrich, Thomas / Lukashev, Evgeny P / Maksimov, Eugene G / Moldenhauer, Marcus / Sluchanko, Nikolai N

Biochimica et biophysica acta. 2020 Feb. 10,

2020

Abstract	Photosynthesis requires various photoprotective mechanisms for survival of organisms in high light. In cyanobacteria exposed to high light, the Orange Carotenoid Protein (OCP) is reversibly photoswitched from the orange (OCPO) to the red (OCPR) form, the latter binds to the antenna (phycobilisomes, PBs) and quenches its overexcitation. OCPR accumulation implicates restructuring of a compact dark-adapted OCPO state including detachment of the N-terminal extension (NTE) and separation of protein domains, which is reversed by interaction with the Fluorescence Recovery Protein (FRP). OCP phototransformation supposedly occurs via an intermediate characterized by an OCPR-like absorption spectrum and an OCPO-like protein structure, but the hierarchy of steps remains debatable. Here, we devise and analyze an OCP variant with the NTE trapped on the C-terminal domain (CTD) via an engineered disulfide bridge (OCPCC). NTE trapping preserves OCP photocycling within the compact protein structure but precludes functional interaction with PBs and especially FRP, which is completely restored upon reduction of the disulfide bridge. Non-interacting with the dark-adapted oxidized OCPCC, FRP binds reduced OCPCC nearly as efficiently as OCPO devoid of the NTE, suggesting that the low-affinity FRP binding to OCPO is realized via NTE displacement. The low efficiency of excitation energy transfer in complexes between PBs and oxidized OCPCC indicates that OCPCC binds to PBs in an orientation suboptimal for quenching PBs fluorescence. Our approach supports the presence of the OCPR-like intermediate in the OCP photocycle and shows effective uncoupling of spectral changes from functional OCP photoactivation, enabling redox control of its structural dynamics and function.
Keywords	amino acid sequences ; carotenoids ; Cyanobacteria ; disulfide bonds ; energy transfer ; fluorescence ; oxidation ; photochemistry ; photosynthesis ; phycobilisome ; protein domains ; radiation resistance ; spectral analysis
Language	English
Dates of publication	2020-0210
Publishing place	Elsevier B.V.
Document type	Article
Note	Pre-press version
ZDB-ID	282711-6
ISSN	0005-2728 ; 0304-4173
ISSN	0005-2728 ; 0304-4173
DOI	10.1016/j.bbabio.2020.148174
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Hybrid complexes of photosynthetic reaction centers and quantum dots in various matrices: resistance to UV irradiation and heating.

Knox, Peter P / Lukashev, Evgeny P / Gorokhov, Vladimir V / Grishanova, Nadezhda P / Paschenko, Vladimir Z

Photosynthesis research

2018 Volume 139, Issue 1-3, Page(s) 295–305

Abstract: The effects of ultraviolet (UV) irradiation (up to 0.6 J/ ... ...

Abstract	The effects of ultraviolet (UV) irradiation (up to 0.6 J/cm
MeSH term(s)	Heating ; Photosynthetic Reaction Center Complex Proteins/metabolism ; Quantum Dots ; Rhodobacter/metabolism ; Trehalose/metabolism ; Ultraviolet Rays
Chemical Substances	Photosynthetic Reaction Center Complex Proteins ; Trehalose (B8WCK70T7I)
Language	English
Publishing date	2018-06-15
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/s11120-018-0529-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

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
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

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)

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Functional interaction of low-homology FRPs from different cyanobacteria with Synechocystis OCP.

Slonimskiy, Yury B / Maksimov, Eugene G / Lukashev, Evgeny P / Moldenhauer, Marcus / Jeffries, Cy M / Svergun, Dmitri I / Friedrich, Thomas / Sluchanko, Nikolai N

Biochimica et biophysica acta. Bioenergetics

2018 Volume 1859, Issue 5, Page(s) 382–393

Abstract: Photosynthesis requires a balance between efficient light harvesting and protection against photodamage. The cyanobacterial photoprotection system uniquely relies on the functioning of the photoactive orange carotenoid protein (OCP) that under intense ... ...

Abstract	Photosynthesis requires a balance between efficient light harvesting and protection against photodamage. The cyanobacterial photoprotection system uniquely relies on the functioning of the photoactive orange carotenoid protein (OCP) that under intense illumination provides fluorescence quenching of the light-harvesting antenna complexes, phycobilisomes. The recently identified fluorescence recovery protein (FRP) binds to the photoactivated OCP and accelerates its relaxation into the basal form, completing the regulatory circle. The molecular mechanism of FRP functioning is largely controversial. Moreover, since the available knowledge has mainly been gained from studying Synechocystis proteins, the cross-species conservation of the FRP mechanism remains unexplored. Besides phylogenetic analysis, we performed a detailed structural-functional analysis of two selected low-homology FRPs by comparing them with Synechocystis FRP (SynFRP). While adopting similar dimeric conformations in solution and preserving binding preferences of SynFRP towards various OCP variants, the low-homology FRPs demonstrated distinct binding stoichiometries and differentially accentuated features of this functional interaction. By providing clues to understand the FRP mechanism universally, our results also establish foundations for upcoming structural investigations necessary to elucidate the FRP-dependent regulatory mechanism.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Phylogeny ; Structural Homology, Protein ; Structure-Activity Relationship ; Synechocystis/chemistry ; Synechocystis/genetics ; Synechocystis/metabolism
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2018-03-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
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.2018.03.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

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
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito