Information on EC 1.10.3.9 - photosystem II

for references in articles please use BRENDA:EC1.10.3.9
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.10.3.9
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RECOMMENDED NAME
GeneOntology No.
photosystem II
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 H2O + 2 plastoquinone + 4 hnu = O2 + 2 plastoquinol
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
photosynthesis light reactions
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Chlorella ohadii
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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PSII is highly sensitive to photoinhibiton in the psbL deletion mutant. The electron flow to plastoquinone in PSII is impaired in the psbJ deletion mutant
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
show the reaction diagram
H2O + 1,4-benzoquinone + hv
O2 + 1,4-benzoquinol
show the reaction diagram
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?
H2O + 2,5-dimethyl-p-benzoquinone + hv
O2 + 2,5-dimethyl-p-benzoquinol
show the reaction diagram
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?
H2O + 2,6-dichloro-4-benzoquinone + hv
O2 + 2,6-dichloro-4-benzoquinol
show the reaction diagram
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?
H2O + 2,6-dichloro-p-benzoquinone + hv
O2 + 2,6-dichloro-p-benzoquinol
show the reaction diagram
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?
H2O + 2,6-dichlorophenolindophenol + hv
O2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
H2O + duroquinone + hv
O2 + duroquinol
show the reaction diagram
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?
H2O + ferricyanide + hv
O2 + ferrocyanide
show the reaction diagram
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?
H2O + phenyl-p-benzoquinone + hv
O2 + phenyl-p-benzoquinol
show the reaction diagram
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?
H2O + plastoquinone + hv
O2 + plastoquinol
show the reaction diagram
O2 + plastoquinol
H2O + plastoquinone + hv
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
show the reaction diagram
H2O + plastoquinone + hv
O2 + plastoquinol
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(3,4-dichlorophenyl)-1,1-dimethylurea
3-[3,4-dichlorophenyl]-1,1-dimethylurea
8-hydroxy-N-(3-methylphenyl)quinoline-2-carboxamide
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digalactosyldiacylglycerol
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minor influence on the reduction kinetics of plastoquinone QA
formate
monogalactosyldiacylglycerol
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minor influence on the reduction kinetics of plastoquinone QA
N-(3-fluorophenyl)-8-hydroxyquinoline-2-carboxamide
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phosphatidylglycerol
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perturbs the intrinsic PSII electron transport, leading to a dissociation of the inner antenna protein CP43 and the 27- and 25-kDa apoproteins of the light-harvesting complex II. Influence is much less than sulfoquinovosyldiacylglycerol
sulfoquinovosyldiacylglycerol
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presence of sulfoquinovosyldiacylglycerol perturbs the intrinsic PSII electron transport significantly, leading to a dissociation of the inner antenna protein CP43 and the 27- and 25-kDa apoproteins of the light-harvesting complex II
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-dinitro-6-sec-butylphenol
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binds to plastoquinone binding site QD, enhances the signal in electron paramagnetic resonance spin-trapping spectroscopy using 5-(ethoxycarbonyl)-5-methyl-1-pyrroline N-oxide but inhibits photoreduction of the high-potential form of cytochrome b559
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
O2
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pH not specified in the publication, temperature not specified in the publication
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.054
plastoquinol
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at 21% O2, pH not specified in the publication, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019
3-(3,4-dichlorophenyl)-1,1-dimethylurea
Spinacia oleracea
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pH not specified in the publication, temperature not specified in the publication
0.0027
8-hydroxy-N-(3-methylphenyl)quinoline-2-carboxamide
Spinacia oleracea
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pH not specified in the publication, temperature not specified in the publication
0.0023
N-(3-fluorophenyl)-8-hydroxyquinoline-2-carboxamide
Spinacia oleracea
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pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.3
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assay at
6.5 - 7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
Thermosynechococcus elongatus (strain BP-1)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
MALDI-TOF mass spectrometry; MALDI-TOF mass spectrometry
multimer
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photosystem II consists of a dimeric photosystem II reaction centre core surrounded by monomeric Lhcb4 (chlorophyll protein 29), Lhcb5 (chlorophyll protein 26) and trimeric light-harvesting complex II antenna proteins
additional information
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PSII structure model analysis, H-bond patterns, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of the X-ray crystallographic structure of the PSII complexe from Thermosynechococcus elongatus at 2.9 A resolution, PDB entry code 3BZ1
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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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
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PSII is inactivated by freezing
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N234D
mutation of residue that interacts with two of the phosphatidylglycerol molecules of the complex. Mutant exhibits normal growth, but shows decreased photosynthetic activities and slower electron transport from QA to QB than the control strain
S232A
mutation of residue that interacts with two of the phosphatidylglycerol molecules of the complex. Mutant exhibits normal growth, but shows decreased photosynthetic activities and slower electron transport from QA to QB than the control strain
S232A/N234D
mutation of residues that interact with two of the phosphatidylglycerol molecules of the complex. Mutant exhibits normal growth, but shows decreased photosynthetic activities and slower electron transport from QA to QB than the control strain. The levels of extrinsic proteins, PsbV and PsbU, are decreased in PSII monomers, while that of Psb28 is increased. The content of phosphatidylglycerol in PSII is slightly decreased, whereas that of monogalactosyldiacylglycerol is increased
S264K
mutation in protein D1. Mutant displays a severe and persistent hampering of the QA-QB electron transfer resulting in a delay of the plastoquinone pool reduction rate
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