Photosystem II

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<StructureSection load='3a0b' size='400' caption='Photosystem II, [[3a0b]]' scene='' >
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<StructureSection load='3a0b' size='350' caption='Photosystem II, [[3a0b]]' scene='' >
==Background==
==Background==
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This structure of '''Photosystem II''' was crystallized from the cyanobacteria, ''Thermosynechococcus elongatus'', at 3.0Å <ref>PMID: 16355230</ref> and at 3.50 Å <ref>PMID: 14764885</ref>. PDB codes are [[2axt]] and [[1s5l]], respectively. Cyanobacteria and plants both contain Photosystem II while photosynthetic bacteria contain the bacterial reaction center. This photosynthetic protein complex is associated with a variety of functional ligands. It is a <scene name='Photosystem_II/Psii_dimer/1'>dimer</scene> composed mainly of alpha-helices. Nineteen <scene name='Photosystem_II/Protein_only/1'>subunits</scene> are in each monomer, with multiple extrinsic subunits associated with the oxygen evolving complex missing from this crystallization. Photosystem II is a membrane bound protein complex that in plants is associated with the thylakoid membrane of chloroplasts. <scene name='Photosystem_II/Hydrophobic_polar/1'>Polar and hydrophobic</scene> regions correlate with membrane associated nature of the protein. '''<FONT COLOR="#616D7E">Hydrophobic</FONT>''' helices make up the transmembranal portion, while '''<FONT COLOR="#C031C7">polar</FONT>''' residues are concentrated externally on either side of the membrane.
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This structure of '''Photosystem II''' was crystallized from the cyanobacteria, ''Thermosynechococcus elongatus'', at 3.0Å <ref>PMID: 16355230</ref> and at 3.50 Å <ref name="Archit">PMID: 14764885</ref>. PDB codes are [[2axt]] and [[1s5l]], respectively. Cyanobacteria and plants both contain Photosystem II while photosynthetic bacteria contain the bacterial reaction center. This photosynthetic protein complex is associated with a variety of functional ligands. It is a <scene name='Photosystem_II/Psii_dimer/1'>dimer</scene> composed mainly of alpha-helices. Nineteen <scene name='Photosystem_II/Protein_only/1'>subunits</scene> are in each monomer, with multiple extrinsic subunits associated with the oxygen evolving complex missing from this crystallization. Photosystem II is a membrane bound protein complex that in plants is associated with the thylakoid membrane of chloroplasts. <scene name='Photosystem_II/Hydrophobic_polar/1'>Polar and hydrophobic</scene> regions correlate with membrane associated nature of the protein. '''<span style="color:gray;background-color:black;font-weight:bold;">Hydrophobic</span>''' helices make up the transmembranal portion, while '''<FONT COLOR="#C031C7">polar</FONT>''' residues are concentrated externally on either side of the membrane.
==Photosynthesis==
==Photosynthesis==
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Photosystem II is an integral part of photosynthesis, the conversion of light energy into chemical energy by living organisms. Photosystem II is linked to a variety of other proteins, including Photosytem I. These proteins ultimately produce NADPH and ATP that power the Calvin cycle. Using this energy, glucose is synthesized from carbon dioxide and water.
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Photosystem II is an integral part of photosynthesis, the conversion of light energy into chemical energy by living organisms. Photosystem II is linked to a variety of other proteins, including Photosytem I. These proteins ultimately produce NADPH and ATP that power the [[Calvin cycle]]. Using this energy, glucose is synthesized from carbon dioxide and water. See also [[Photosynthesis]].
==Electron Transfer==
==Electron Transfer==
[[Image:Chlorophyll_a.svg.png|thumb|170px|left|structure of chlorophyll ''a'']]
[[Image:Chlorophyll_a.svg.png|thumb|170px|left|structure of chlorophyll ''a'']]
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<scene name='Photosystem_II/Chlorophyll_green/4'>Chlorophyll</scene> surround Photosystem II and capture energy from sunlight, exciting electrons. Chlorophyll are highly conjugated and absorb visible light, along with accessory light harvesting pigments such as <scene name='Photosystem_II/Betacarotene/3'>beta carotene</scene>. Beta carotene absorbs visible light of other wavelengths and also protects Photosystem II by destroying reactive oxygen species that result from this photoexcitation. Electrons are passed from chlorophyll to <scene name='Photosystem_II/Pheophytin_purple/5'>pheophytin</scene>. Pheophytin are very similar to chlorophyll except they contain 2 H<sup>+</sup> instead of a Mg<sup>2+</sup> ion. From the pheophytin, electrons transferred to <scene name='Photosystem_II/Quinone_pink/5'>plastoquinones</scene>, which are reduced. Located between each pair of quinones, an iron helps to transfer the electron. These plastoquinones eventually move to a plastoquinone pool which travels to another large protein subunit, cytochrome b <sub>6</sub>/ f. Eventually these electrons reduce NADP<sup>+</sup> to NADPH. The <scene name='Photosystem_II/Electron_pathway/3'>electron pathway</scene> through Photosystem II is shown, with '''<FONT COLOR="#F87217">beta-carotenes</FONT>''', '''<FONT COLOR="#571B7e">pheophytins</FONT>''', '''<FONT COLOR="#E42217">iron</FONT>''' and '''<FONT COLOR="#F535AA">plasotoquinones</FONT>'''.
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<scene name='Photosystem_II/Chlorophyll_green/4'>Chlorophyll</scene> surround Photosystem II and capture energy from sunlight, exciting electrons. Chlorophyll are highly conjugated and absorb visible light, along with accessory light harvesting pigments such as <scene name='Photosystem_II/Betacarotene/3'>beta carotene</scene>. Beta carotene absorbs visible light of other wavelengths and also protects Photosystem II by destroying reactive oxygen species that result from this photoexcitation. Electrons are passed from chlorophyll to <scene name='Photosystem_II/Pheophytin_purple/5'>pheophytin</scene>. Pheophytin are very similar to chlorophyll except they contain 2 H<sup>+</sup> instead of a Mg<sup>2+</sup> ion. From the pheophytin, electrons transferred to <scene name='Photosystem_II/Quinone_pink/5'>plastoquinones</scene>, which are reduced. Located between each pair of quinones, an iron helps to transfer the electron. These plastoquinones eventually move to a plastoquinone pool which travels to another large protein subunit, cytochrome b <sub>6</sub>/ f. Eventually these electrons reduce NADP<sup>+</sup> to NADPH. The <scene name='Photosystem_II/Electron_pathway/3'>electron pathway</scene> through Photosystem II is shown, with '''<span style="color:orange;background-color:black;font-weight:bold;">beta-carotenes</span>''', '''<FONT COLOR="#571B7e">pheophytins</FONT>''', '''<FONT COLOR="#E42217">iron</FONT>''' and '''<FONT COLOR="#F535AA">plasotoquinones</FONT>'''.
{{Clear}}
{{Clear}}
==Oxygen Evolution==
==Oxygen Evolution==
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Another important facet of Photosystem II is its ability to oxidize water to oxygen with its <scene name='Photosystem_II/Oxygen_evolving_centers/11'>oxygen evolving centers</scene>. These centers are <scene name='Photosystem_II/Single_oxygen_evolving/1'>cubane-like</scene> structures with 3 '''<FONT COLOR="#8D38C9">manganese</FONT>''', 4 '''<FONT COLOR="#C11B17">oxygen</FONT>''' and a '''<FONT COLOR="#59E817">calcium</FONT>''' linked to a fourth manganese<ref>PMID: 14764885</ref>. Oxidation of water leaves 2 H <sup>+</sup> on the lumenal side of the membrane, helping to establish the proton gradient essential for ATP synthesis in the CF<sub>1</sub>CF<sub>0</sub>-ATP sythase protein.
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Another important facet of Photosystem II is its ability to oxidize water to oxygen with its <scene name='Photosystem_II/Oxygen_evolving_centers/11'>oxygen evolving centers</scene>. These centers are <scene name='Photosystem_II/Single_oxygen_evolving/1'>cubane-like</scene> structures with 3 '''<FONT COLOR="#8D38C9">manganese</FONT>''', 4 '''<FONT COLOR="#C11B17">oxygen</FONT>''' and a '''<span style="color:lime;background-color:black;font-weight:bold;">calcium</span>''' linked to a fourth manganese<ref name="Archit" />. Oxidation of water leaves 2 H <sup>+</sup> on the lumenal side of the membrane, helping to establish the proton gradient essential for ATP synthesis in the CF<sub>1</sub>CF<sub>0</sub>-ATP sythase protein.
[[Image:b-car.svg.png|b-car.svg.png|thumb|left|400px|structure of beta carotene]]
[[Image:b-car.svg.png|b-car.svg.png|thumb|left|400px|structure of beta carotene]]
[[Image:plastoquinone.jpg|thumb|300px|left|reduced plastoquinone]]
[[Image:plastoquinone.jpg|thumb|300px|left|reduced plastoquinone]]
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</StructureSection>
 
==3D structures of photosystem II==
==3D structures of photosystem II==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[Photosystem II 3D structures]]
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[[3arc]], [[3a0b]], [[3a0h]], [[4il6]], [[3wu2]], [[4ub6]], [[4ub8]] – PSII – ''Thermosynechococcus vulcanos''<br />
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</StructureSection>
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[[3prq]], [[3prr]] - TePSII + terbutryn – ''Thermosynechococcus elongatus''<br />
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[[3kzi]], [[3bz1]], [[3bz2]], [[2axt]], [[1w5c]], [[1s5l]], [[1izl]], [[1ilx]], [[1fe1]], [[4fby]], [[4ixr]], [[4ixq]], [[4pbu]], [[4pj0]], [[4q54]], [[4tnh]], [[4tni]], [[4tnj]], [[4tnk]] – TePSII<br />
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[[3zpn]] - TePSII PSB28 protein<br />
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[[4k7b]] - PSII extrinsic protein – ''Chaetoceros gracilis''<br />
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[[2y6x]] – TePSII PSB27 protein<br />
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[[2kvo]] – SyPSII reaction center PSB28 protein – Synechocystis – NMR<br />
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[[2kmf]], [[2knd]] - SyPSII reaction center PSB27 subunit – NMR<br />
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[[2vu4]], [[1vyk]], [[4rti]] – spPSII PSBP subunit – spinach<br />
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[[1nze]] - spPSII PSBQ subunit<br />
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[[1v2b]] - PSII PSBP subunit – tobacco<br />
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[[4rth]] - PSII PSBP subunit – maize<br />
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[[1fc6]], [[1fc7]], [[1fc9]], [[1fcf]] – PSII C terminal processing protease – ''Scenedesmus obliquus''
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==Additional Resources==
==Additional Resources==

Current revision

Photosystem II, 3a0b

Drag the structure with the mouse to rotate

Additional Resources

For additional information, see: Photosynthesis

References

  1. Loll B, Kern J, Saenger W, Zouni A, Biesiadka J. Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II. Nature. 2005 Dec 15;438(7070):1040-4. PMID:16355230 doi:http://dx.doi.org/10.1038/nature04224
  2. 2.0 2.1 Ferreira KN, Iverson TM, Maghlaoui K, Barber J, Iwata S. Architecture of the photosynthetic oxygen-evolving center. Science. 2004 Mar 19;303(5665):1831-8. Epub 2004 Feb 5. PMID:14764885 doi:http://dx.doi.org/10.1126/science.1093087
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