Photosynthetic Reaction Center Complex Proteins
"Photosynthetic Reaction Center Complex Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II.
| Descriptor ID |
D045322
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| MeSH Number(s) |
D05.500.562.488 D08.811.600.710 D12.776.543.930.500 D12.776.765.199.750.750
|
| Concept/Terms |
|
Below are MeSH descriptors whose meaning is more general than "Photosynthetic Reaction Center Complex Proteins".
Below are MeSH descriptors whose meaning is more specific than "Photosynthetic Reaction Center Complex Proteins".
This graph shows the total number of publications written about "Photosynthetic Reaction Center Complex Proteins" by people in this website by year, and whether "Photosynthetic Reaction Center Complex Proteins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1999 | 1 | 0 | 1 |
| 2000 | 1 | 0 | 1 |
| 2001 | 1 | 0 | 1 |
| 2002 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
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Below are the most recent publications written about "Photosynthetic Reaction Center Complex Proteins" by people in Profiles.
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Photosynthetic reaction center mimicry of a "special pair" dimer linked to electron acceptors by a supramolecular approach: self-assembled cofacial zinc porphyrin dimer complexed with fullerene(s). Chemistry. 2007; 13(3):916-22.
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Key role of proline L209 in connecting the distant quinone pockets in the reaction center of Rhodobacter sphaeroides. Proc Natl Acad Sci U S A. 2002 May 14; 99(10):6702-6.
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Revealing the involvement of extended hydrogen bond networks in the cooperative function between distant sites in bacterial reaction centers. J Biol Chem. 2001 Dec 07; 276(49):45513-5.
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Modeling the effects of mutations on the free energy of the first electron transfer from QA- to QB in photosynthetic reaction centers. Biochemistry. 2000 May 23; 39(20):5940-52.
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Calculated protein and proton motions coupled to electron transfer: electron transfer from QA- to QB in bacterial photosynthetic reaction centers. Biochemistry. 1999 Jun 29; 38(26):8253-70.