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<title>Photosystem II</title>

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Photosystem II

</h1>

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</style><div role="note" class="hatnote navigation-not-searchable">"PSII" redirects here. For the video game console, see <a href="PlayStation_2" title="PlayStation 2">PlayStation 2</a>. For the Indonesian political party, see <a href="Indonesian_Islamic_Union_Party" title="Indonesian Islamic Union Party">Indonesian Islamic Union Party</a>. For other uses, see <a href="PS2_(disambiguation)" class="mw-disambig" title="PS2 (disambiguation)">PS2 (disambiguation)</a>.</div>

Photosystem II (or water-plastoquinone oxidoreductase) is the first <a href="Protein_complex" title="Protein complex">protein complex</a> in the <a href="Light-dependent_reactions" title="Light-dependent reactions">light-dependent reactions</a> of oxygenic <a href="Photosynthesis" title="Photosynthesis">photosynthesis</a>. It is located in the <a href="Thylakoid_membrane" class="mw-redirect" title="Thylakoid membrane">thylakoid membrane</a> of <a href="Plants" class="mw-redirect" title="Plants">plants</a>, <a href="Algae" title="Algae">algae</a>, and <a href="Cyanobacteria" title="Cyanobacteria">cyanobacteria</a>. Within the photosystem, <a href="Enzyme" title="Enzyme">enzymes</a> capture <a href="Photons" class="mw-redirect" title="Photons">photons</a> of light to energize <a href="Electrons" class="mw-redirect" title="Electrons">electrons</a> that are then transferred through a variety of <a href="Coenzymes" class="mw-redirect" title="Coenzymes">coenzymes</a> and <a href="Cofactor_(biochemistry)" title="Cofactor (biochemistry)">cofactors</a> to reduce <a href="Plastoquinone" title="Plastoquinone">plastoquinone</a> to plastoquinol. The energized electrons are replaced by <a href="Oxidizing" class="mw-redirect" title="Oxidizing">oxidizing</a> water to form <a href="Hydrogen_ions" class="mw-redirect" title="Hydrogen ions">hydrogen ions</a> and molecular oxygen.

By replenishing lost electrons with electrons from the <a href="Photodissociation" title="Photodissociation">splitting of water</a>, photosystem II provides the electrons for all of photosynthesis to occur. The hydrogen ions (protons) generated by the oxidation of water help to create a <a href="Proton_gradient" class="mw-redirect" title="Proton gradient">proton gradient</a> that is used by <a href="ATP_synthase" title="ATP synthase">ATP synthase</a> to generate <a href="Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>. The energized electrons transferred to plastoquinone are ultimately used to reduce NADP+ to <a href="NADPH" class="mw-redirect" title="NADPH">NADPH</a> or are used in <a href="Light-dependent_reactions" title="Light-dependent reactions">non-cyclic electron flow</a>.<a href="#cite_note-1">[1]</a> <a href="DCMU" title="DCMU">DCMU</a> is a chemical often used in laboratory settings to inhibit photosynthesis. When present, DCMU inhibits electron flow from photosystem II to plastoquinone.

<div class="mw-heading mw-heading2"><h2 id="Structure_of_complex">Structure of complex</h2></div>

The core of PSII consists of a pseudo-symmetric heterodimer of two homologous proteins D1 and D2.<a href="#cite_note-Rutherford2003-2">[2]</a> Unlike the reaction centers of all other <a href="Photosystem" title="Photosystem">photosystems</a> in which the positive charge sitting on the chlorophyll dimer that undergoes the initial photoinduced charge separation is equally shared by the two monomers, in intact PSII the charge is mostly localized on one chlorophyll center (70−80%).<a href="#cite_note-3">[3]</a> Because of this, P680+ is highly oxidizing and can take part in the splitting of water.<a href="#cite_note-Rutherford2003-2">[2]</a>

Photosystem II (of <a href="Cyanobacteria" title="Cyanobacteria">cyanobacteria</a> and green plants) is composed of around 20 subunits (depending on the organism) as well as other accessory, light-harvesting proteins. Each photosystem II contains at least 99 cofactors: 35 chlorophyll a, 12 <a href="Beta-carotene" class="mw-redirect" title="Beta-carotene">beta-carotene</a>, two <a href="Pheophytin" title="Pheophytin">pheophytin</a>, two <a href="Plastoquinone" title="Plastoquinone">plastoquinone</a>, two <a href="Heme" title="Heme">heme</a>, one bicarbonate, 20 lipids, the Mn 4CaO 5 cluster (including two chloride ions), one non heme Fe2+ and two putative Ca2+ ions per monomer.<a href="#cite_note-Guskov09-4">[4]</a> There are several crystal structures of photosystem II.<a href="#cite_note-5">[5]</a> The <a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a> accession codes for this protein are <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=3WU2">3WU2</a>, <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=3BZ1">3BZ1</a>, <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=3BZ2">3BZ2</a> (3BZ1 and 3BZ2 are monomeric structures of the Photosystem II dimer),<a href="#cite_note-Guskov09-4">[4]</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2AXT">2AXT</a>, <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1S5L">1S5L</a>, <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1W5C">1W5C</a>, <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ILX">1ILX</a>, <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1FE1">1FE1</a>, <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1IZL">1IZL</a>.

<caption>Protein Subunits (only with known function)

</caption>

<th>Subunit

</th>

<th>Family

</th>

<th>Function

</th></tr>

<tr>

<td>D1 (PsbA)

</td>

<td rowspan="2"><a href="Photosynthetic_reaction_centre_protein_family" title="Photosynthetic reaction centre protein family">Photosynthetic reaction centre protein family</a>

</td>

<td>Reaction center protein, binds Chlorophyll P680, pheophytin, beta-carotene, quinone and manganese center

</td></tr>

<tr>

<td>D2 (PsbD)

</td>

<td>Reaction center protein

</td></tr>

<tr>

<td>CP43 (PsbC)

</td>

<td rowspan="2"><a href="Photosystem_II_light-harvesting_protein" title="Photosystem II light-harvesting protein">Photosystem II light-harvesting protein</a>

</td>

<td>Binds manganese center

</td></tr>

<tr>

<td>CP47 (PsbB)

</td>

<td>

</td></tr>

<tr>

<td>O

</td>

<td>Manganese-stabilising protein (<a href="InterPro" title="InterPro">InterPro</a>: <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/interpro/entry/IPR002628">IPR002628</a>)

</td>

<td>Manganese Stabilizing Protein

</td></tr>

<tr>

<td style="text-align:center" colspan="3">By convention, gene names are formed by Psb + subunit letter. For example, subunit O is PsbO. The exceptions are D1 (PsbA) and D2 (PsbD).

</td></tr></tbody></table>

<caption>Coenzymes/Cofactors

</caption>

<th>Cofactor

</th>

<th>Function

</th></tr>

<tr>

<td><a href="Chlorophyll" title="Chlorophyll">Chlorophyll</a>

</td>

<td>Absorbs light energy and converts it to chemical energy

</td></tr>

<tr>

<td><a href="Beta-carotene" class="mw-redirect" title="Beta-carotene">Beta-carotene</a>

</td>

<td>Quench excess photoexcitation energy

</td></tr>

<tr>

<td><a href="Heme_B" title="Heme B">Heme B</a>559

</td>

<td>Bound to <a href="Cytochrome_b559" title="Cytochrome b559">Cytochrome b559</a> (PsbE–PsbF) as a secondary/protective electron carrier

</td></tr>

<tr>

<td><a href="Pheophytin" title="Pheophytin">Pheophytin</a>

</td>

<td>Primary electron acceptor

</td></tr>

<tr>

<td><a href="Plastoquinone" title="Plastoquinone">Plastoquinone</a>

</td>

<td>Mobile intra-thylakoid membrane electron carrier

</td></tr>

<tr>

<td><a href="Oxygen-evolving_complex" title="Oxygen-evolving complex">Manganese center</a>

</td>

<td>Also known as the oxygen evolving center, or OEC

</td></tr></tbody></table>

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</style><table class="infobox"><tbody><tr><th colspan="2" class="infobox-above">Photosystem II</th></tr><tr><th colspan="2" class="infobox-header" style="background-color: light-dark(#ddd, #404244) !important; color:inherit;">Identifiers</th></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit;"><a href="Enzyme_Commission_number" title="Enzyme Commission number">EC no.</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><a rel="nofollow" class="external text" href="https://www.enzyme-database.org/query.php?ec=1.10.3.9">1.10.3.9</a></td></tr><tr><th colspan="2" class="infobox-header" style="background-color: light-dark(#ddd, #404244) !important; color:inherit;">Databases</th></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit;"><a href="IntEnz" title="IntEnz">IntEnz</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=1.10.3.9">IntEnz view</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit;"><a href="BRENDA" title="BRENDA">BRENDA</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><a rel="nofollow" class="external text" href="http://www.brenda-enzymes.org/enzyme.php?ecno=1.10.3.9">BRENDA entry</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit;"><a href="ExPASy" class="mw-redirect" title="ExPASy">ExPASy</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><a rel="nofollow" class="external text" href="https://enzyme.expasy.org/EC/1.10.3.9">NiceZyme view</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit;"><a href="KEGG" title="KEGG">KEGG</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><a rel="nofollow" class="external text" href="https://www.genome.jp/dbget-bin/www_bget?enzyme+1.10.3.9">KEGG entry</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit;"><a href="MetaCyc" title="MetaCyc">MetaCyc</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><a rel="nofollow" class="external text" href="https://biocyc.org/META/substring-search?type=NIL&object=1.10.3.9">metabolic pathway</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit;"><a href="PRIAM_enzyme-specific_profiles" title="PRIAM enzyme-specific profiles">PRIAM</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><a rel="nofollow" class="external text" href="http://priam.prabi.fr/cgi-bin/PRIAM_profiles_CurrentRelease.pl?EC=1.10.3.9">profile</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit;"><a href="Protein_Data_Bank" title="Protein Data Bank">PDB</a> structures</th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><a rel="nofollow" class="external text" href="https://www.rcsb.org/search?q=rcsb_polymer_entity.rcsb_ec_lineage.id:1.10.3.9">RCSB PDB</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/entry/search/index?ec_number:1.10.3.9">PDBe</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/enzymes/GetPage.pl?ec_number=1.10.3.9">PDBsum</a></td></tr><tr><td colspan="2" class="infobox-full-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit;"><table class="infobox mw-collapsible mw-collapsed" style="float:none; clear:none; margin:0; border-width:0; border-collapse:collapse; text-align:left; width:100%"><tbody><tr><th colspan="2" class="infobox-header" style="background-color: light-dark(#ddd, #404244) !important; color:inherit;">Search</th></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit; border:light-dark(#f8f9fa, #202122) 2px solid !important; border-width:3px 2px 0 0;"><a href="PubMed_Central" title="PubMed Central">PMC</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit; border:light-dark(#f8f9fa, #202122) 2px solid !important; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&term=1.10.3.9%5BEC/RN%20Number%5D%20AND%20pubmed%20pmc%20local%5Bsb%5D">articles</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit; border:light-dark(#f8f9fa, #202122) 2px solid !important; border-width:3px 2px 0 0;"><a href="PubMed" title="PubMed">PubMed</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit; border:light-dark(#f8f9fa, #202122) 2px solid !important; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&term=1.10.3.9%5BEC/RN%20Number%5D">articles</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: light-dark(#e7dcc3, #3b3018) !important; color:inherit; border:light-dark(#f8f9fa, #202122) 2px solid !important; border-width:3px 2px 0 0;"><a href="National_Center_for_Biotechnology_Information" title="National Center for Biotechnology Information">NCBI</a></th><td class="infobox-data" style="background-color: light-dark(#eee, #27292d) !important; color:inherit; border:light-dark(#f8f9fa, #202122) 2px solid !important; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/protein?term=1.10.3.9%5BEC/RN%20Number%5D">proteins</a></td></tr></tbody></table></td></tr></tbody></table>

<div class="mw-heading mw-heading2"><h2 id="Oxygen-evolving_complex_(OEC)">Oxygen-evolving complex (OEC)</h2></div>

<div role="note" class="hatnote navigation-not-searchable">Main article: <a href="Oxygen-evolving_complex" title="Oxygen-evolving complex">oxygen-evolving complex</a></div>

The oxygen-evolving complex is the site of water oxidation. It is a metallo-oxo cluster comprising four manganese ions (in oxidation states ranging from +3 to +4)<a href="#cite_note-6">[6]</a> and one divalent calcium ion. When it oxidizes water, producing oxygen gas and protons, it sequentially delivers the four electrons from water to a tyrosine (D1-Y161) sidechain and then to P680 itself. It is composed of three protein subunits, OEE1 (PsbO), OEE2 (PsbP) and OEE3 (PsbQ); a fourth PsbR peptide is associated nearby.

The first structural model of the oxygen-evolving complex was solved using <a href="X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a> from frozen protein crystals with a resolution of 3.8<a href="%C3%85ngstr%C3%B6m" class="mw-redirect" title="Ångström">Å</a> in 2001.<a href="#cite_note-7">[7]</a> Over the next years the resolution of the model was gradually increased to 2.9<a href="%C3%85ngstr%C3%B6m" class="mw-redirect" title="Ångström">Å</a>.<a href="#cite_note-8">[8]</a><a href="#cite_note-9">[9]</a><a href="#cite_note-10">[10]</a> While obtaining these structures was in itself a great feat, they did not show the oxygen-evolving complex in full detail. In 2011 the OEC of PSII was resolved to a level of 1.9Å revealing five oxygen atoms serving as oxo bridges linking the five metal atoms and four water molecules bound to the Mn 4CaO 5 cluster; more than 1,300 water molecules were found in each photosystem II monomer, some forming extensive hydrogen-bonding networks that may serve as channels for protons, water or oxygen molecules.<a href="#cite_note-pmid21499260-11">[11]</a> At this stage, it is suggested that the structures obtained by <a href="X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a> are biased, since there is evidence that the manganese atoms are reduced by the high-intensity <a href="X-rays" class="mw-redirect" title="X-rays">X-rays</a> used, altering the observed OEC structure. This incentivized researchers to take their crystals to a different X-ray facilities, called <a href="X-ray_free-electron_laser" class="mw-redirect" title="X-ray free-electron laser">X-ray Free Electron Lasers</a>, such as <a href="SLAC_National_Accelerator_Laboratory" title="SLAC National Accelerator Laboratory">SLAC</a> in the USA. In 2014 the structure observed in 2011 was confirmed.<a href="#cite_note-12">[12]</a> Knowing the structure of Photosystem II did not suffice to reveal how it works exactly. So now the race has started to solve the structure of Photosystem II at different stages in the mechanistic cycle (discussed below). Currently structures of the S1 state and the S3 state's have been published almost simultaneously from two different groups, showing the addition of an oxygen molecule designated O6 between Mn1 and Mn4,<a href="#cite_note-13">[13]</a><a href="#cite_note-14">[14]</a> suggesting that this may be the site on the oxygen evolving complex, where oxygen is produced.

<div class="mw-heading mw-heading2"><h2 id="Water_splitting">Water splitting</h2></div>

Photosynthetic water splitting (or <a href="Oxygen_evolution" title="Oxygen evolution">oxygen evolution</a>) is one of the most important reactions on the planet, since it is the source of nearly all the atmosphere's oxygen. Moreover, artificial photosynthetic water-splitting may contribute to the effective use of sunlight as an alternative energy source.

The mechanism of water oxidation is understood in substantial detail.<a href="#cite_note-15">[15]</a><a href="#cite_note-16">[16]</a><a href="#cite_note-17">[17]</a> The oxidation of water to molecular oxygen requires extraction of four electrons and four protons from two molecules of water. The experimental evidence that oxygen is released through cyclic reaction of oxygen evolving complex (OEC) within one PSII was provided by Pierre Joliot et al.<a href="#cite_note-18">[18]</a> They have shown that, if dark-adapted photosynthetic material (higher plants, algae, and cyanobacteria) is exposed to a series of single turnover flashes, oxygen evolution is detected with typical period-four damped oscillation with maxima on the third and the seventh flash and with minima on the first and the fifth flash (for review, see<a href="#cite_note-19">[19]</a>). Based on this experiment, Bessel Kok and co-workers <a href="#cite_note-20">[20]</a> introduced a cycle of five flash-induced transitions of the so-called S-states, describing the four redox states of OEC: When four oxidizing equivalents have been stored (at the S4-state), OEC returns to its basic S0-state. In the absence of light, the OEC will "relax" to the S1 state; the S1 state is often described as being "dark-stable". The S1 state is largely considered to consist of manganese ions with oxidation states of Mn3+, Mn3+, Mn4+, Mn4+.<a href="#cite_note-:0-21">[21]</a> Finally, the intermediate S-states<a href="#cite_note-22">[22]</a> were proposed by Jablonsky and Lazar as a regulatory mechanism and link between S-states and tyrosine Z.

In 2012, Renger expressed the idea of internal changes of water molecules into typical oxides in different S-states during water splitting.<a href="#cite_note-23">[23]</a>

<div class="mw-heading mw-heading2"><h2 id="Inhibitors">Inhibitors</h2></div>

<a href="Enzyme_inhibitor" title="Enzyme inhibitor">Inhibitors</a> of PSII are used as herbicides. There are two main chemical families, the <a href="1%2C3%2C5-Triazine" title="1,3,5-Triazine">triazines</a> derived from <a href="Cyanuric_chloride" title="Cyanuric chloride">cyanuric chloride</a><a href="#cite_note-24">[24]</a> of which <a href="Atrazine" title="Atrazine">atrazine</a> and <a href="Simazine" title="Simazine">simazine</a> are the most commonly used and the <a href="Aryl" class="mw-redirect" title="Aryl">aryl</a> <a href="Ureas" title="Ureas">ureas</a> which include <a href="Chlortoluron" title="Chlortoluron">chlortoluron</a> and <a href="Diuron" class="mw-redirect" title="Diuron">diuron</a> (DCMU).<a href="#cite_note-25">[25]</a><a href="#cite_note-26">[26]</a>

<ul><li><a href="Oxygen_evolution" title="Oxygen evolution">Oxygen evolution</a></li>

<li><a href="Photosynthesis" title="Photosynthesis">Photosynthesis</a></li>

<li><a href="Photosystem" title="Photosystem">Photosystem</a></li>

<li><a href="Photosystem_I" title="Photosystem I">Photosystem I</a></li>

<li><a href="Photosystem_II_light-harvesting_protein" title="Photosystem II light-harvesting protein">Photosystem II light-harvesting protein</a></li>

<li><a href="Reaction_Centre" class="mw-redirect" title="Reaction Centre">Reaction Centre</a></li>

<li><a href="Photoinhibition" title="Photoinhibition">Photoinhibition</a></li></ul>

<div class="mw-heading mw-heading2"><h2 id="References">References</h2></div>

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<li id="cite_note-18"><a href="#cite_ref-18">^</a> <cite id="CITEREFJoliot_P.Barbieri_G.Chabaud_R.1969" class="citation journal cs1">Joliot P.; Barbieri G.; Chabaud R. (1969). "Un nouveau modele des centres photochimiques du systeme II". Photochemistry and Photobiology. 10 (5): 309–329. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1751-1097.1969.tb05696.x">10.1111/j.1751-1097.1969.tb05696.x</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:96744015">96744015</a>.</cite>

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<li id="cite_note-19"><a href="#cite_ref-19">^</a> <cite id="CITEREFJoliot2003" class="citation journal cs1">Joliot P (2003). "Period-four oscillations of the flash-induced oxygen formation in photosynthesis". Photosynthesis Research. 76 (1–3): 65–72. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1023%2FA%3A1024946610564">10.1023/A:1024946610564</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16228566">16228566</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:8742213">8742213</a>.</cite>

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<li id="cite_note-20"><a href="#cite_ref-20">^</a> <cite id="CITEREFKokForbushMcGloin1970" class="citation journal cs1">Kok B, Forbush B, McGloin M (June 1970). "Cooperation of charges in photosynthetic O2 evolution-I. A linear four step mechanism". Photochemistry and Photobiology. 11 (6): 457–75. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1751-1097.1970.tb06017.x">10.1111/j.1751-1097.1970.tb06017.x</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/5456273">5456273</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:31914925">31914925</a>.</cite>

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<li id="cite_note-:0-21"><a href="#cite_ref-:0_21-0">^</a> <cite id="CITEREFKuntzlemanYocum2005" class="citation journal cs1">Kuntzleman T, Yocum CF (February 2005). "Reduction-induced inhibition and Mn(II) release from the photosystem II oxygen-evolving complex by hydroquinone or NH2OH are consistent with a Mn(III)/Mn(III)/Mn(IV)/Mn(IV) oxidation state for the dark-adapted enzyme". Biochemistry. 44 (6): 2129–42. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fbi048460i">10.1021/bi048460i</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15697239">15697239</a>.</cite>

</li>

<li id="cite_note-22"><a href="#cite_ref-22">^</a> <cite id="CITEREFJablonskyLazar2008" class="citation journal cs1">Jablonsky J, Lazar D (April 2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2267143">"Evidence for intermediate S-states as initial phase in the process of oxygen-evolving complex oxidation"</a>. Biophysical Journal. 94 (7): 2725–36. <a href="Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2008BpJ....94.2725J">2008BpJ....94.2725J</a>. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1529%2Fbiophysj.107.122861">10.1529/biophysj.107.122861</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2267143">2267143</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18178650">18178650</a>.</cite>

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<li id="cite_note-23"><a href="#cite_ref-23">^</a> <cite id="CITEREFRenger2012" class="citation journal cs1">Renger G (August 2012). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bbabio.2012.02.005">"Mechanism of light induced water splitting in Photosystem II of oxygen evolving photosynthetic organisms"</a>. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817 (8): 1164–76. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bbabio.2012.02.005">10.1016/j.bbabio.2012.02.005</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22353626">22353626</a>.</cite>

</li>

<li id="cite_note-24"><a href="#cite_ref-24">^</a> <cite class="citation web cs1"><a rel="nofollow" class="external text" href="http://www.alanwood.net/pesticides/class_herbicides.html#chlorotriazine_herbicides">"Chlorotraizine herbicides"</a>. alanwood.net. Retrieved 2021-03-26.</cite>

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<li id="cite_note-25"><a href="#cite_ref-25">^</a> <cite class="citation web cs1"><a rel="nofollow" class="external text" href="http://www.alanwood.net/pesticides/class_herbicides.html#urea_herbicides">"Urea herbicides"</a>. alanwood.net. Retrieved 2021-03-26.</cite>

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<li id="cite_note-26"><a href="#cite_ref-26">^</a> <cite id="CITEREFOettmeier1992" class="citation book cs1">Oettmeier W (1992). "Herbicides of photosystem II". The Photosystems. pp. 349–408. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FB978-0-444-89440-3.50018-7">10.1016/B978-0-444-89440-3.50018-7</a>. <a href="ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <bdi>9780444894403</bdi>.</cite>

</li>

</ol></div>

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</style><div id="Oxidoreductases:_diphenol_family_(EC_1.10)386" style="font-size:114%;margin:0 4em"><a href="Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a>: <a href="Benzenediol" class="mw-redirect" title="Benzenediol">diphenol</a> family (<a href="Enzyme_Commission_number" title="Enzyme Commission number">EC</a> 1.10)</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="List_of_EC_numbers_(EC_1)#EC_1.10.1_With_NAD_or_NADP_as_acceptor" title="List of EC numbers (EC 1)">1.10.1</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Trans-acenaphthene-1%2C2-diol_dehydrogenase" title="Trans-acenaphthene-1,2-diol dehydrogenase">Trans-acenaphthene-1,2-diol dehydrogenase</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="List_of_EC_numbers_(EC_1)#EC_1.10.2_With_a_cytochrome_as_acceptor" title="List of EC numbers (EC 1)">1.10.2</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Coenzyme_Q_%E2%80%93_cytochrome_c_reductase" title="Coenzyme Q – cytochrome c reductase">Coenzyme Q - cytochrome c reductase</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="List_of_EC_numbers_(EC_1)#EC_1.10.3_With_oxygen_as_acceptor" title="List of EC numbers (EC 1)">1.10.3</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Catechol_oxidase" title="Catechol oxidase">Catechol oxidase</a></li>

<li><a href="Laccase" title="Laccase">Laccase</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="List_of_EC_numbers_(EC_1)#EC_1.10.99_With_other_acceptors" title="List of EC numbers (EC 1)">1.10.99</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Cytochrome_b6f_complex" title="Cytochrome b6f complex">Cytochrome b6f complex</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Alternative_oxidase" title="Alternative oxidase">Alternative oxidase</a></li></ul>

</div></td></tr></tbody></table></div>

<div class="navbox-styles"></div><div role="navigation" class="navbox" aria-labelledby="Enzymes56" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Enzymes56" style="font-size:114%;margin:0 4em"><a href="Enzyme" title="Enzyme">Enzymes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Activity</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Active_site" title="Active site">Active site</a></li>

<li><a href="Binding_site" title="Binding site">Binding site</a></li>

<li><a href="Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li>

<li><a href="Oxyanion_hole" title="Oxyanion hole">Oxyanion hole</a></li>

<li><a href="Enzyme_promiscuity" title="Enzyme promiscuity">Enzyme promiscuity</a></li>

<li><a href="Diffusion-limited_enzyme" title="Diffusion-limited enzyme">Diffusion-limited enzyme</a></li>

<li><a href="Cofactor_(biochemistry)" title="Cofactor (biochemistry)">Cofactor</a></li>

<li><a href="Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Regulation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Allosteric_regulation" title="Allosteric regulation">Allosteric regulation</a></li>

<li><a href="Cooperativity" title="Cooperativity">Cooperativity</a></li>

<li><a href="Enzyme_inhibitor" title="Enzyme inhibitor">Enzyme inhibitor</a></li>

<li><a href="Enzyme_activator" title="Enzyme activator">Enzyme activator</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Classification</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Enzyme_Commission_number" title="Enzyme Commission number">EC number</a></li>

<li><a href="Protein_superfamily" title="Protein superfamily">Enzyme superfamily</a></li>

<li><a href="Protein_family" title="Protein family">Enzyme family</a></li>

<li><a href="List_of_enzymes" title="List of enzymes">List of enzymes</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Kinetics</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li>

<li><a href="Eadie%E2%80%93Hofstee_diagram" title="Eadie–Hofstee diagram">Eadie–Hofstee diagram</a></li>

<li><a href="Hanes%E2%80%93Woolf_plot" title="Hanes–Woolf plot">Hanes–Woolf plot</a></li>

<li><a href="Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk plot</a></li>

<li><a href="Michaelis%E2%80%93Menten_kinetics" title="Michaelis–Menten kinetics">Michaelis–Menten kinetics</a></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li>EC1 <a href="Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a> (<a href="List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li>

<li>EC2 <a href="Transferase" title="Transferase">Transferases</a> (<a href="List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li>

<li>EC3 <a href="Hydrolase" title="Hydrolase">Hydrolases</a> (<a href="List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li>

<li>EC4 <a href="Lyase" title="Lyase">Lyases</a> (<a href="List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li>

<li>EC5 <a href="Isomerase" title="Isomerase">Isomerases</a> (<a href="List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li>

<li>EC6 <a href="Ligase" title="Ligase">Ligases</a> (<a href="List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li>

<li>EC7 <a href="Translocase" title="Translocase">Translocases</a> (<a href="List_of_EC_numbers_(EC_7)" title="List of EC numbers (EC 7)">list</a>)</li></ul>

</div></td></tr></tbody></table></div>

<div class="navbox-styles"></div><div role="navigation" class="navbox" aria-labelledby="Enzymes:_multienzyme_complexes94" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Enzymes:_multienzyme_complexes94" style="font-size:114%;margin:0 4em"><a href="Enzyme" title="Enzyme">Enzymes</a>: <a href="Protein_complex" title="Protein complex">multienzyme complexes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Photosynthesis" title="Photosynthesis">Photosynthesis</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Photosynthetic_reaction_centre" title="Photosynthetic reaction centre">Photosynthetic reaction center complex proteins</a></li>

<li><a href="Photosystem" title="Photosystem">Photosystem</a>

</ul></li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Dehydrogenase" title="Dehydrogenase">Dehydrogenase</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="2-oxoadipate_dehydrogenase_complex" title="2-oxoadipate dehydrogenase complex">2-oxoadipate dehydrogenase complex</a>

<ul><li><a href="DHTKD1" title="DHTKD1">DHTKD1</a></li>

<li><a href="Branched-chain_alpha-keto_acid_dehydrogenase_complex" title="Branched-chain alpha-keto acid dehydrogenase complex">Branched-chain alpha-keto acid dehydrogenase complex</a>

<ul><li><a href="BCKDHA" title="BCKDHA">BCKDHA</a></li>

<li><a href="BCKDHB" title="BCKDHB">BCKDHB</a></li>

<li><a href="Pyruvate_dehydrogenase_complex" title="Pyruvate dehydrogenase complex">Pyruvate dehydrogenase complex</a>

<li><a href="Oxoglutarate_dehydrogenase_complex" title="Oxoglutarate dehydrogenase complex">Oxoglutarate dehydrogenase</a>

<ul><li><a href="Carbamoyl_phosphate_synthase_II" title="Carbamoyl phosphate synthase II">Carbamoyl phosphate synthase II</a></li>

<li><a href="Aspartate_carbamoyltransferase" title="Aspartate carbamoyltransferase">Aspartate carbamoyltransferase</a></li>

<li><a href="Dihydroorotase" title="Dihydroorotase">Dihydroorotase</a></li></ul></li>

<li><a href="P450-containing_systems" title="P450-containing systems">P450-containing systems</a></li>

<li><a href="Cytochrome_b6f_complex" title="Cytochrome b6f complex">Cytochrome b6f complex</a></li>

<li><a href="Electron_transport_chain" title="Electron transport chain">Electron transport chain</a></li>

<li><a href="Fatty_acid_synthase" title="Fatty acid synthase">Fatty acid synthetase complex</a></li>

<li><a href="Glycine_cleavage_system" title="Glycine cleavage system">Glycine decarboxylase complex</a></li>

<li><a href="Mitochondrial_trifunctional_protein" title="Mitochondrial trifunctional protein">Mitochondrial trifunctional protein</a>

<ul><li><a href="HADHA" title="HADHA">HADHA</a></li>

<li><a href="HADHB" title="HADHB">HADHB</a></li></ul></li>

<li><a href="PEP_group_translocation" title="PEP group translocation">Phosphoenolpyruvate sugar phosphotransferase system</a></li>

<li><a href="Polyketide_synthase" title="Polyketide synthase">Polyketide synthase</a></li>

<li><a href="Sucrase-isomaltase" title="Sucrase-isomaltase">Sucrase-isomaltase complex</a></li>

<li><a href="Tryptophan_synthase" title="Tryptophan synthase">Tryptophan synthase</a></li></ul>

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This article is issued from <a class="external text" title="Last edited on 2025-05-23" href="https://en.wikipedia.org/wiki/?title=Photosystem_II&oldid=1291839733">Wikipedia</a>. The text is available under <a class="external text" href="https://creativecommons.org/licenses/by-sa/4.0/deed.en">Creative Commons Attribution-Share Alike 4.0</a> unless otherwise noted. Additional terms may apply for the media files.

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