| Name | CP47 |
|---|---|
| Synonyms | 49 kDa cytoskeletal protein; BFSP 2; BFSP2; Beaded filament structural protein 2; CP 47; CP47; CP49; LIFL L… |
| Name | diuron |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 7635157 | Zer H, Ohad I: Photoinactivation of photosystem II induces changes in the photochemical reaction center II abolishing the regulatory role of the QB site in the D1 protein degradation. Eur J Biochem. 1995 Jul 15;231(2):448-53. The effect of 3-(3,4-dichlorophenyl)-1,1-dimethyl urea (diuron) binding at the secondary (QB) binding site of reaction center II (RCII), on the high-light-induced degradation of the RCII proteins D1 and D2, and the core proteins CP43 and CP47 was investigated in vivo in Chlamydomonas reinhardtii. |
81(1,1,1,1) | Details |
| 8980503 | Wu J, Putnam-Evans C, Bricker TM: Site-directed mutagenesis of the CP 47 protein of photosystem II: 167W in the lumenally exposed loop C is required for photosystem II assembly and stability. Plant Mol Biol. 1996 Nov;32(3):537-42. |
4(0,0,0,4) | Details |
| 8494886 | Shen G, Eaton-Rye JJ, Vermaas WF: Mutation of residues in CP47 leads to destabilization of the photosystem II complex and to impairment of light energy transfer. Biochemistry. 1993 May 18;32(19):5109-15. |
4(0,0,0,4) | Details |
| 12552150 | Suzuki T, Minagawa J, Tomo T, Sonoike K, Ohta H, Enami I: Binding and functional properties of the extrinsic proteins in -evolving photosystem II particle from a green alga, Chlamydomonas reinhardtii having his-tagged CP47. Plant Cell Physiol. 2003 Jan;44(1):76-84. |
2(0,0,0,2) | Details |
| 11598237 | Ruffle SV, Wang J, Johnston HG, Gustafson TL, Hutchison RS, Minagawa J, Crofts A, Sayre RT: Photosystem II peripheral accessory chlorophyll mutants in Chlamydomonas reinhardtii. Plant Physiol. 2001 Oct;127(2):633-44. These Chls are axially coordinated by the D1-H118 and D2-H117 residues and are in close association with the proximal Chl antennae proteins, CP43 and CP47. |
1(0,0,0,1) | Details |
| 6373796 | Camm EL, Green BR: Isolation of PS II reaction centre and its relationship to the minor chlorophyll-protein complexes. J Cell Biochem. 1983;23(1-4):171-9. Evidence is presented for the identification of the chlorophyll- protein complex CPa-1 (CP 47) as the reaction centre of photosystem II (PS II). |
1(0,0,0,1) | Details |
| 8219045 | Kuhn MG, Vermaas WF: Deletion mutations in a long hydrophilic loop in the photosystem II chlorophyll-binding protein CP43 in the cyanobacterium Synechocystis sp. Plant Mol Biol. 1993 Oct;23(1):123-33. CP47, the other major chlorophyll-binding protein, was present in reduced but significant amounts in the thylakoid. Herbicide binding (diuron) was lost in all but one mutant indicating the PSII components are not assembled into functionally intact complexes. |
1(0,0,0,1) | Details |
| 9711300 | Xiong J, Minagawa J, Crofts A, Govindjee: Loss of inhibition by in newly constructed photosystem II D1 mutants, D1-R257E and D1-R257M, of Chlamydomonas reinhardtii. Biochim Biophys Acta. 1998 Jul 20;1365(3):473-91. Additional effects on the donor side cannot yet be excluded. (4) The binding affinity for the herbicide DCMU is unaltered. (5) The mutants grow photosynthetically, but at a decreased (approximately 70% of the wild type) level. (6) The Fo level was elevated (approximately 40-50%) which could be due to a decrease in the excitation energy transfer from the antenna to the PSII reaction center, and/or to an increased level of [QA-] in the dark. (7) A decreased (approximately 10%) ratio of F685 (mainly from CP43) and F695 (mainly from CP47) to F715 (mainly from PSI) emission bands at 77 K suggests a change in the antenna complex. |
1(0,0,0,1) | Details |
| 18777103 | Rose S, Minagawa J, Seufferheld M, Padden S, Svensson B, Kolling DR, Crofts AR, Govindjee: D1-arginine257 mutants (R257E, K, and Q) of Chlamydomonas reinhardtii have a lowered QB redox potential: analysis of thermoluminescence and fluorescence measurements. Photosynth Res. 2008 Oct-Dec;98(1-3):449-68. Epub 2008 Sep 6. We discuss an indirect mechanism mediated through electrostatic and/or surface charge effects and the possibility of more pleiotropic effects arising from decreased stability of the D1/D2 and D1/CP47 interfaces. |
1(0,0,0,1) | Details |