Any feedback?
No. of entries
Information on EC 1.10.3.9 - photosystem II
for references in articles please use BRENDA:EC1.10.3.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.10 Acting on diphenols and related substances as donors
1.10.3 With oxygen as acceptor
1.10.3.9 photosystem II
IUBMB Comments
Contains chlorophyll a, β-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.
The enzyme appears in viruses and cellular organisms
- 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
showSynonyms
photosystem ii, psba2, oxygen-evolving photosystem ii, psba1, water:plastoquinone oxidoreductase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PSII
PSII
Thermosynechococcus vestitus 34-H
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 H2O + 2 plastoquinone + 4 hnu = O2 + 2 plastoquinol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
photosynthesis light reactions, protective electron sinks in the thylakoid membrane (PSII to PTOX)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
H2O + 1,4-benzoquinone + hv
O2 + 1,4-benzoquinol
-
Substrates: -
Products: -
Products: -
?
H2O + 2,5-dimethyl-p-benzoquinone + hv
O2 + 2,5-dimethyl-p-benzoquinol
-
Substrates: -
Products: -
Products: -
?
H2O + 2,6-dichloro-4-benzoquinone + hv
O2 + 2,6-dichloro-4-benzoquinol
-
Substrates: -
Products: -
Products: -
?
H2O + 2,6-dichloro-p-benzoquinone + hv
O2 + 2,6-dichloro-p-benzoquinol
-
Substrates: -
Products: -
Products: -
?
H2O + phenyl-p-benzoquinone + hv
O2 + phenyl-p-benzoquinol
-
Substrates: -
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
-
Substrates: -
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
-
Substrates: 2,6-dichloro-1,4-benzoquinone and K3Fe(CN)6 as electron acceptors. Oxidation of free quinols by one-electron carriers proceeds rather slowly
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
Substrates: -
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
Substrates: photosystem II splits water and drives electron transfer to plastoquinone via photochemical reactions using light energy
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
-
Substrates: -
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
-
Substrates: -
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
-
Substrates: illumination of spinach PSII membranes deprived of intrinsic plastoquinone results in 1O2 formation, singlet oxygen scavenging activity of plastoquinol in photosystem II, significantly suppressed by addition of exogenous plastoquinol to plastoquinone-depleted PSII membranes. Presence of exogenous plastoquinols with a different side-chain length causes a similar extent of 1O2 scavenging activity
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
Thermostichus vulcanus
-
Substrates: -
Products: -
Products: -
?
H2O + 2,6-dichlorophenolindophenol + hv
O2 + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
H2O + 2,6-dichlorophenolindophenol + hv
O2 + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
H2O + plastoquinone + hv
O2 + plastoquinol
-
Substrates: -
Products: -
Products: -
?
H2O + plastoquinone + hv
O2 + plastoquinol
-
Substrates: -
Products: -
Products: -
?
H2O + plastoquinone + hv
O2 + plastoquinol
Thermosynechococcus vestitus
-
Substrates: -
Products: -
Products: -
?
H2O + plastoquinone + hv
O2 + plastoquinol
Thermosynechococcus vestitus
Substrates: -
Products: -
Products: -
?
H2O + plastoquinone + hv
O2 + plastoquinol
Thermosynechococcus vestitus
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: PS II membrane fragments that contain a membrane pool of PQ and are largely devoid of PS I and Cyt b6f complexes are a convenient object to investigate the process of Cyt b559 photoreduction: biphasic reduction of cytochrome b559 by plastoquinol in photosystem II membrane fragments, two types of cytochrome b559/plastoquinone redox equilibria, detailed overview. In samples of PS II membrane fragments with preoxidized Cyt b559 only a fraction of Cyt b559 (about a half of photoreduced Cyt b559) can be rapidly reduced following a short illumination while the other reduced Cyt b559 is accumulated much slower in the dark. Photoreduction of Cyt b559 in the presence of decylplastoquinone
Products: -
Products: -
?
additional information
?
-
-
Substrates: application of electron acceptors from PSII, 2,6-dimethylbenzoquinone and,2,6-dichlorophenolindophenol, to measure PSII activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: PS II proteins PsbL and PsbJ regulate electron flow to the plastoquinone pool
Products: -
Products: -
?
additional information
?
-
-
Substrates: plastoquinone functions as the primary electron acceptor of photosystem II and beta-carotene does not play a direct role in the primary photochemistry but is required for the C-550 absorbance change
Products: -
Products: -
?
additional information
?
-
-
Substrates: the O2 radical anion is formed via the reduction of molecular oxygen by plastosemiquinones formed through one-electron reduction of plastoquinone at the quinone binding site QB and one-electron oxidation of plastoquinol by Cyt b559 at the QC site
Products: -
Products: -
?
additional information
?
-
Thermosynechococcus vestitus
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Thermosynechococcus vestitus
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
-
Substrates: -
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
Substrates: photosystem II splits water and drives electron transfer to plastoquinone via photochemical reactions using light energy
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
-
Substrates: -
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
-
Substrates: -
Products: -
Products: -
?
2 H2O + 2 plastoquinone + 4 hv
O2 + 2 plastoquinol
Thermostichus vulcanus
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Thermostichus vulcanus
-
photosystem II uses light to drive water oxidation and plastoquinone reduction. Plastoquinone reduction involves two PQ cofactors, QA and QB, working in series. QA is a one-electron carrier, whereas QB undergoes sequential reduction and protonation to form QBH2. QBH2 exchanges with plastoquinone from the pool in the membrane
-
additional information
-
Raman spectroscopy of plastoquinone in PSII membrane shows prominent vibrational signals The signals of cofactors QA and QB can be distinguished. The redox potential difference is about a 86 mV
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
digalactosyldiacylglycerol
-
minor influence on the reduction kinetics of plastoquinone QA
monogalactosyldiacylglycerol
-
minor influence on the reduction kinetics of plastoquinone QA
phosphatidylglycerol
-
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
-
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
3-(3,4-dichlorophenyl)-1,1-dimethylurea
-
binds to plastoquinone binding site QB, 50% inhibition of signal in electron paramagnetic resonance spin-trapping spectroscopy using 5-(ethoxycarbonyl)-5-methyl-1-pyrroline N-oxide and inhibits photoreduction of the high-potential form of cytochrome b559
3-[3,4-dichlorophenyl]-1,1-dimethylurea
-
stress factor inhibiting photosynthesis
formate
Thermostichus vulcanus
-
formate ligation to Fe2+ does not significantly affect the protonation of reduced Q, Fe2+ inhibits QBH2 release rather than its formation
additional information
-
light-induced oxidative stress leads to photoinactivation of the oxygen-evolving photosystem II. In contrast to model organisms, photosynthesis persists in Microcoleus sp. even at light intensities 2-3times higher than required to saturate oxygen evolution. This is despite an extensive loss (85-90%) of variable fluorescence and thermoluminescence, representing radiative PSII charge recombination that promotes the generation of damaging singlet oxygen. Light induced loss of variable fluorescence is not inhibited by the electron transfer inhibitors 3-(3,4-dichlorophenyl)-1,1-dimethylurea, 2,5-dibromo-3-methyl-6-isopropylbenzoquinone, nor the uncoupler carbonyl cyanide-p-trifluoromethoxyphenylhydrazone, thus indicating that reduction of plastoquinone or O2, or lumen acidification essential for non-photochemical quenching are not involved
-
additional information
-
inhibitory efficiency of ring-substituted 8-hydroxyquinoline-2-carboxanilides depends on the compound lipophilicity, the electronic properties of the substituent R and the position of the substituent R on the benzene ring. Compounds probably bind the section between P680 and plastoquinone QB on the acceptor side of PS II
-
additional information
-
under UV-B stress, none of the D1 isoforms is significantly induced or accumulates. UV-B stress leads to changes in electron flow on the acceptor side of the PSII complex resulting from an increased redox potential gap between QA and plastoquinone pool.
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-dinitro-6-sec-butylphenol
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
O2
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
plastoquinone kinetic behaviour of reaction centres under dark and light adapted conditions, chlorophyll fluorescence measurements, overview
-
additional information
additional information
-
plastoquinone kinetic behaviour of reaction centres under dark and light adapted conditions, chlorophyll fluorescence measurements, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.054
plastoquinol
-
at 21% O2, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
3-(3,4-dichlorophenyl)-1,1-dimethylurea
Spinacia oleracea
-
pH not specified in the publication, temperature not specified in the publication
0.0027
8-hydroxy-N-(3-methylphenyl)quinoline-2-carboxamide
Spinacia oleracea
-
pH not specified in the publication, temperature not specified in the publication
0.0023
N-(3-fluorophenyl)-8-hydroxyquinoline-2-carboxamide
Spinacia oleracea
-
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P07753: photosystem II protein D1, P06007: photosystem II D2 protein
SwissProt
brenda
-
-
-
brenda
Thermosynechococcus vestitus
wild type and mutant viridis zb63 lacking photosystem I but with normal photosystem II activity
-
-
brenda
cytochrome b559 subunit alpha, photosystem II reaction center subunit V
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
presence of monogalactosyldiacylglycerol leads to a dimerization of isolated, monomeric PSII core complexes. Presence of sulfoquinovosyldiacylglycerol and phosphatidylglycerol induce a detachment of CP43 from the PSII core, thereby disturbing the intrinsic PSII electron transport
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
-
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
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
malfunction
Thermosynechococcus vestitus 34-H
-
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
-
physiological function
-
there are two distinct signalling pathways activated by excess light absorbed by photosystem II: one, dependent on the redox state of the electron transport chain, is involved in the regulation of antenna size, and the second, more directly linked to the level of photoinhibitory stress perceived by the cell, participates in regulating carotenoid biosynthesis
physiological function
-
photosystem II is a light-driven water-plastoquinone oxidoreductase. It produces molecular oxygen as an enzymatic product. Under a variety of stress conditions, reactive oxygen species are produced at or near the active site for oxygen evolution
physiological function
Thermostichus vulcanus
-
photosystem II uses light to drive water oxidation and plastoquinone reduction. Plastoquinone reduction involves two PQ cofactors, QA and QB, working in series. QA is a one-electron carrier, whereas QB undergoes sequential reduction and protonation to form QBH2.QBH2 exchanges with plastoquinone from the pool in the membrane
physiological function
-
a darkadapted mutant lacking terminal oxidases with naturally reduced plastoquinone is characterized by slower QA-roxidation and O2 evolution rates and lower quantum yield of PSII primary photochemical reactions as compared to the wild type and succinate dehydrogenaselacking mutant, in which the plastoquinone pool remains oxidized in the dark. Light adaptation increases PSII primary photochemical reactions in all tested strains, with the greatest increase in in the mutant. Continuous illumination of mutant cells with low intensity blue light also increases PSII primary photochemical reactions and PSII functional absorption crosssection. This effect is almost absent in the wild type and succinate dehydrogenaselacking mutant
physiological function
-
cells grow increasingly faster at higher light intensities from low to high to extreme by escalating photoprotection via shifting from linear electron flow (PSII-LEF) to cyclic electron flow (PSII-CEF) with concomitant PSII charge separation from plastoquinone reduction (PSII-LEF) to plastoquinol oxidation (PSII-CEF). Low light-grown cells have unusually small antennae, use mainly PSII-LEF and convert 40% of PSII charge separations into O2. High light-grown cells have smaller antenna and lower PSII-LEF. Extreme light-grown cells have no LHCII antenna, minimal PSII-LEF, and a doubling time of 1.3 h
physiological function
Thermostichus vulcanus
-
molecular dynamics simulations of PSII embedded in the thylakoid membrane. In addition to the two known channels, a third channel for plastoquinone/plastoquinone diffusion is observed between the thylakoid membrane and the plastoquinone binding sites. In a promiscuous diffusion mechanism all three channels function as entry and exit channels. The exchange cavity serves as a plastoquinone reservoir
physiological function
-
redox heterogeneity of the native population of Cyt b559 is due to heme-quinone redox interactions. The interacting plastoquinone is caged in the protein interior in the singly protonated state. The model of redox interaction successfully explains the singularity of Cyt b559 among heme proteins, its redox heterogeneity, the atypically high Em value of the high potential form, the large difference in the Em values between the redox forms, and the instability of the heme protein towards mild treatments
physiological function
-
the cyclic electron transport (CET) around photosystem PS II is an alternative electron transport pathway. Under N limitation, the activity of the cyclic electron transport by PSII is increased and linearly correlated with the amount of alternative electron transport rates. Cyclic electron transport by PSII is activated already at the end of the dark period under N-limited conditions and coincides with a significantly increased degree of reduction of the plastoquinone pool. A carbon allocation in favor of carbohydrates occurs during the light period and their degradation during the dark phase
physiological function
-
the extent of reduction of the plastoquinone pool in the photosynthetic electron transport chain increases with an increase in illumination intensity during growth, the effective quantum yield of photosynthesis decreases. During the adaptation the size of the antenna decreases, correlating with a decrease in the amounts of proteins of peripheral pigment-protein complexes due to suppression of gene transcription. The quantum yield of photosynthesis is restored
physiological function
photosystem II splits water and drives electron transfer to plastoquinone via photochemical reactions using light energy
physiological function
-
the extent of reduction of the plastoquinone pool in the photosynthetic electron transport chain increases with an increase in illumination intensity during growth, the effective quantum yield of photosynthesis decreases. During the adaptation the size of the antenna decreases, correlating with a decrease in the amounts of proteins of peripheral pigment-protein complexes due to suppression of gene transcription. The quantum yield of photosynthesis is restored
-
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
additional information
-
identification of oxidized amino acid residues in the D1, D2 CP47, and CP43 proteins, in the vicinity of the Mn4O5Ca cluster active site of PS II, by mass spectrometry. The residues are modified by reactive oxygen species generated within the PS II complex
additional information
Thermostichus vulcanus
-
mechanism of proton-coupled quinone reduction in photosystem II, overview. The initial proton transfer to QB.- occurs from the protonated, D1-His252 to QB.- via D1-Ser264. The second proton transfer is likely to occur from D1-His215 to QBH- via an H-bond with an energy profile with a single well, resulting in the formation of QBH2 and the D1-His215 anion. The pathway for reprotonation of D1-His215- may involve bicarbonate, D1-Tyr246 and water in the QB site. Potential-energy profiles of the H-bond donor-acceptor pairs, overview
additional information
-
plastoquinol exogenously added to plastoquinone-depleted PSII membranes serves as efficient scavenger of 1O2, overview
Show AA Sequence and Transmembrane Helices (26580 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermosynechococcus vestitus BP-1