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Information on EC 1.10.3.9 - photosystem II and Organism(s) Thermosynechococcus vestitus and UniProt Accession P0A444
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1.10.3.9 photosystem IIIUBMB Comments
Contains chlorophyll a, beta-carotene, pheophytin, plastoquinone, a Mn4Ca cluster, heme and non-heme iron. Four successive photoreactions, resulting in a storage of four positive charges, are required to oxidize two water molecules to one oxygen molecule.
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Word Map
- 1.10.3.9
- chlorophyll
- chloroplast
- thylakoids
-
photochemical
-
light-harvesting
- antenna
-
photoinhibition
- spinach
- cyanobacterium
- illumination
- synechocystis
- co2
-
dissipation
-
photoprotection
-
photochemistry
-
non-photochemical
- qa
- manganese
- epr
-
light-induced
-
acclimation
-
photon
- lhcii
- reinhardtii
-
stomatal
- flash
-
carotenoid
-
extrinsic
- chlamydomonas
-
photodamage
-
herbicide
-
supercomplexes
- synechococcus
-
dark-adapted
- elongatus
- zeaxanthin
-
singlet
-
pigment-protein
-
photoautotrophic
-
xanthophyl
- photooxidation
-
solar
-
phytoplankton
-
photoinactivation
-
excitonic
- atrazine
-
photoreduction
- plastocyanin
-
far-red
-
light-driven
The enzyme appears in selected viruses and cellular organisms
Synonyms
photosystem ii, psba2, oxygen-evolving photosystem ii, psba1, water:plastoquinone oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PSII
SYSTEMATIC NAME
IUBMB Comments
H2O:plastoquinone reductase (light-dependent)
Contains chlorophyll a, beta-carotene, pheophytin, plastoquinone, a Mn4Ca cluster, heme and non-heme iron. Four successive photoreactions, resulting in a storage of four positive charges, are required to oxidize two water molecules to one oxygen molecule.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
H2O + plastoquinone + hv
O2 + plastoquinol
Thermosynechococcus vestitus
-
-
-
?
H2O + plastoquinone + hv
O2 + plastoquinol
Thermosynechococcus vestitus
-
-
-
?
H2O + plastoquinone + hv
O2 + plastoquinol
Thermosynechococcus vestitus
-
photosystem II catalyzes the light-induced transfer of electrons from water to plastoquinone accompanied by the net transport of protons from the cytoplasm (stroma) to the lumen, the production of molecular oxygen and the release of plastoquinol into the membrane phase
-
-
?
additional information
?
-
Thermosynechococcus vestitus
photosystem II is a large homdimeric protein-cofactor complex consisting of 20 protein subunits, 35 chlorophyll a molecules and 12 carotenoid molecules, 25 integral lipids and 1 chloride ion per monomer
-
-
?
additional information
?
-
Thermosynechococcus vestitus
photosystem II is a large homdimeric protein-cofactor complex consisting of 20 protein subunits, 35 chlorophyll a molecules and 12 carotenoid molecules, 25 integral lipids and 1 chloride ion per monomer
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
photosystem II has two bound plastoquinones, QA and QB, which act as sequential electron acceptors. QA is tightly bound and acts as a one electron carrier while QB undergoes two sequential one-electron reduction steps
-
-
?
additional information
?
-
Thermosynechococcus vestitus
photosystem II is a large homdimeric protein-cofactor complex consisting of 20 protein subunits, 35 chlorophyll a molecules and 12 carotenoid molecules, 25 integral lipids and 1 chloride ion per monomer
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
Mn2+
Ca2+
Thermosynechococcus vestitus
-
the enzyme possesses a Mn4Ca cluster, PSII can be inactivated through the depletion of Ca2+ or through loss of the Mn4Ca cluster
Fe2+
Thermosynechococcus vestitus
-
a high spin non-heme iron (Fe2+) is located between the two bound quinones QA and QB
Mn2+
Thermosynechococcus vestitus
-
the enzyme possesses a Mn4Ca cluster, PSII can be inactivated through loss of the Mn4Ca cluster
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Thermosynechococcus vestitus
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
Thermosynechococcus vestitus
-
in the purified photosystem II lacking the PsbJ subunit (DELTAPsbJ-PSII) an active Mn4CaO5 cluster is present in 60-70% of the centers. In these centers, although the forward electron transfer seems not affected, the Em of the secondary quinone acceptor QB/QB(-) couple increases by more than 120 mV , thus disfavoring the electron coming back on primary quinone acceptor QA. The increase of the energy gap between QA/QA(-) and QB/QB(-) could contribute in a protection against the charge recombination between the donor side and QB(-), identified at the origin of photoinhibition under low light, and possibly during the slow photoactivation process
additional information
Thermosynechococcus vestitus
-
calculations at the molecular orbital-MP2/6-31G level using PSII models deduced from the X-ray structure of the PSII complexes from Thermosynechococcus elongatus, molecular interactions of the quinone electron acceptors QA, QB, and QC in photosystem II by the fragment molecular orbital method, arrangement of electron-transfer cofactors in PSII, modelling, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
multimer
Thermosynechococcus vestitus
-
photosystem II (PSII), the oxygen-evolving enzyme, consists of 17 trans-membrane and 3 extrinsic membrane proteins. Other subunits bind to PSII during assembly, like Psb27, Psb28, and Tsl0063
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulations of the complete PSII complex embedded in a lipid bilayer. PSII in the presence of plastoquinol shows a distinct dynamic behaviour which causes disruption of the interactions seen in the PSII-plastoquinone complex and leads to release of plastoquinol from the binding pocket. Displacement of plastoquinol closes the second water channel. Residue D1-Ser264 has a pivotal role in modulating the dynamics of the plastoquinone binding pocket and plastoquinol-plastoquinone exchange via its interaction with residue D1-His252
Thermosynechococcus vestitus
analysis of the X-ray crystallographic structure of the PSII complexe from Thermosynechococcus elongatus at 2.9 A resolution, PDB entry code 3BZ1
Thermosynechococcus vestitus
-
modeling of the binding of lipoprotein Psb27 to the PSII surface in a region that is occupied by subunit PsbV in the mature complex. Psb27 is localized on the PSII surface adjacent to the large lumenal domain of light-harvesting protein CP43. Additional contacts associate Psb27 with light-harvesting protein CP47 and the C-termini of subunits PsbA and PsbB
Thermosynechococcus vestitus
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sedoud, A.; Kastner, L.; Cox, N.; El-Alaoui, S.; Kirilovsky, D.; Rutherford, A.W.
Effects of formate binding on the quinone-iron electron acceptor complex of photosystem II
Biochim. Biophys. Acta
1807
216-226
2011
Thermosynechococcus vestitus
Mueh, F.; Gloeckner, C.; Hellmich, J.; Zouni, A.
Light-induced quinone reduction in photosystem II
Biochim. Biophys. Acta
1817
44-65
2011
Thermosynechococcus vestitus
Guskov, A.; Kern, J.; Gabdulkhakov, A.; Broser, M.; Zouni, A.; Saenger, W.
Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride
Nat. Struct. Mol. Biol.
16
334-342
2009
Thermosynechococcus vestitus (P0A444), Thermosynechococcus vestitus (Q8CM25)
Hasegawa, K.; Noguchi, T.
Molecular interactions of the quinone electron acceptors QA, QB, and QC in photosystem II as studied by the fragment molecular orbital method
Photosynth. Res.
120
113-123
2014
Thermosynechococcus vestitus
Cormann, K.U.; Moeller, M.; Nowaczyk, M.M.
Critical assessment of protein cross-linking and molecular docking an updated model for the interaction between photosystem II and Psb27
Front. Plant Sci.
7
157
2016
Thermosynechococcus vestitus (Q8DG60)
Zobnina, V.; Lambreva, M.D.; Rea, G.; Campi, G.; Antonacci, A.; Scognamiglio, V.; Giardi, M.T.; Polticelli, F.
The plastoquinol-plastoquinone exchange mechanism in photosystem II insight from molecular dynamics simulations
Photosynth. Res.
131
15-30
2017
Thermosynechococcus vestitus (P0A444)
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