Photosystem II

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[[Image:1s5l.gif|250px|left]]
[[Image:1s5l.gif|250px|left]]
==Background==
==Background==
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This structure of Photosystem II was crystallized from the cyanobacteria, ''Thermosynechococcus elongatus'', at 3.0Å <ref>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, 438: 1040-1044. PMID: [http://www.ncbi.nlm.nih.gov/pubmed/16355230 16355230]</ref> and at 3.50 Å (<ref>Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J., Iwata, S. "Architecture of the photosynthetic oxygen-evolving center." Science, March 19, 2004, 303 (5665), 1831-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14764885 14764885]</ref>. PDB codes are [http://www.proteopedia.org/wiki/index.php/2AXT 2AXT] and [http://www.proteopedia.org/wiki/index.php/1S5L 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>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, 438: 1040-1044. PMID: [http://www.ncbi.nlm.nih.gov/pubmed/16355230 16355230]</ref> and at 3.50 Å <ref>Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J., Iwata, S. "Architecture of the photosynthetic oxygen-evolving center." Science, March 19, 2004, 303 (5665), 1831-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14764885 14764885]</ref>. PDB codes are [http://www.proteopedia.org/wiki/index.php/2AXT 2AXT] and [http://www.proteopedia.org/wiki/index.php/1S5L 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.
==Photosynthesis==
==Photosynthesis==

Revision as of 11:53, 7 August 2008

PDB ID 1s5l

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Image:1s5l.gif

Contents

Background

This structure of Photosystem II was crystallized from the cyanobacteria, Thermosynechococcus elongatus, at 3.0Å [1] and at 3.50 Å [2]. 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 composed mainly of alpha-helices. Nineteen 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. regions correlate with membrane associated nature of the protein. Hydrophobic helices make up the transmembranal portion, while polar residues are concentrated externally on either side of the membrane.

Photosynthesis

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.

Electron Transfer

PDB ID 1s5l

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structure of chlorophyll a
structure of chlorophyll a
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 . Beta carotene absorbs visible light of other wavelengths and also protects Photosystem II by destroying reactive oxygen species that result from this photoexcitation.
structure of beta carotene
structure of beta carotene
Electrons are passed from chlorophyll to . Pheophytin are very similar to chlorophyll except they contain 2 H+ instead of a Mg2+ ion. From the pheophytin, electrons transferred to , which are reduced. Between each pair of quinones, an iron, in red, helps to transfer the electron. These plastoquinones eventually move to a plastoquinone pool which travels to another large protein subunit, cytochrome b 6/ f. Eventually these electrons reduce NADP+ to NADPH. The through Photosystem II is shown, with beta-carotenes, pheophytins, iron and plasotoquinones.
reduced plastoquinone
reduced plastoquinone

Oxygen Evolution

Another important facet of Photosystem II is its ability to oxidize water to oxygen with its . These centers are structures with 3 manganese, 4 oxygen and a calcium linked to a fourth manganese.[3] Oxidation of water leaves 2 H + on the lumenal side of the membrane, helping to establish the proton gradient essential for ATP synthesis in the CF1CF0-ATP sythase protein.

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, 438: 1040-1044. PMID: 16355230
  2. ↑ Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J., Iwata, S. "Architecture of the photosynthetic oxygen-evolving center." Science, March 19, 2004, 303 (5665), 1831-8. PMID:14764885
  3. ↑ Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J., Iwata, S. "Architecture of the photosynthetic oxygen-evolving center." Science, March 19, 2004, 303 (5665), 1831-8. PMID:14764885

2. Garrett, R.H., Grisham, C.M. Biochemistry, 3rd Edition. Belmont, CA: Thomson Brooks/ Cole, 2005.

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