| pubmed-article:18777103 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18777103 | lifeskim:mentions | umls-concept:C0085356 | lld:lifeskim |
| pubmed-article:18777103 | lifeskim:mentions | umls-concept:C2003888 | lld:lifeskim |
| pubmed-article:18777103 | lifeskim:mentions | umls-concept:C0242485 | lld:lifeskim |
| pubmed-article:18777103 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:18777103 | lifeskim:mentions | umls-concept:C0016315 | lld:lifeskim |
| pubmed-article:18777103 | lifeskim:mentions | umls-concept:C1709375 | lld:lifeskim |
| pubmed-article:18777103 | lifeskim:mentions | umls-concept:C1272755 | lld:lifeskim |
| pubmed-article:18777103 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:18777103 | pubmed:issue | 1-3 | lld:pubmed |
| pubmed-article:18777103 | pubmed:dateCreated | 2008-12-10 | lld:pubmed |
| pubmed-article:18777103 | pubmed:abstractText | Arginine257 (R257), in the de-helix that caps the Q(B) site of the D1 protein, has been shown by mutational studies to play a key role in the sensitivity of Photosystem II (PS II) to bicarbonate-reversible binding of the formate anion. In this article, the role of this residue has been further investigated through D1 mutations (R257E, R257Q, and R257K) in Chlamydomonas reinhardtii. We have investigated the activity of the Q(B) site by studying differences from wild type on the steady-state turnover of PS II, as assayed through chlorophyll (Chl) a fluorescence yield decay after flash excitation. The effects of p-benzoquinone (BQ, which oxidizes reduced Q(B), Q(B)(-) ) and 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU, which blocks electron flow from Q(A)(-) to Q(B)) were measured. The equilibrium constants of the two-electron gate were obtained through thermoluminescence measurements. The thermoluminescence properties were changed in the mutants, especially when observed after pretreatment with 100 microM BQ. A theoretical analysis of the thermoluminescence data, based mainly on the recombination pathways model of Rappaport et al. (2005), led to the conclusion that the free-energy difference for the recombination of Q(B)(-) with S(2) was reduced by 20-40 mV in the three mutants (D1-R257K, D1-R257Q, and D1-R257E); this was interpreted to be due to a lowering of the redox potential of Q(B)/Q(B)(-). Further, since the recombination of Q(A)(-) with S(2) was unaffected, we suggest that no significant change in redox potential of Q(A)/Q(A)(-) occurred in these three mutants. The maximum variable Chl a fluorescence yield is lowered in the mutants, in the order R257K > R257Q > R257E, compared to wild type. Our analysis of the binary oscillations in Chl a fluorescence following pretreatment of cells with BQ showed that turnover of the Q(B) site was relatively unaffected in the three mutants. The mutant D1-R257E had the lowest growth rate and steady-state activity and showed the weakest binary oscillations. We conclude that the size and the charge of the amino acid at the position D1-257 play a role in PS II function by modulating the effective redox potential of the Q(B)/Q(B)(-) pair. 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. | lld:pubmed |
| pubmed-article:18777103 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18777103 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18777103 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18777103 | pubmed:issn | 0166-8595 | lld:pubmed |
| pubmed-article:18777103 | pubmed:author | pubmed-author:Govindjee | lld:pubmed |
| pubmed-article:18777103 | pubmed:author | pubmed-author:CroftsAntony... | lld:pubmed |
| pubmed-article:18777103 | pubmed:author | pubmed-author:MinagawaJunJ | lld:pubmed |
| pubmed-article:18777103 | pubmed:author | pubmed-author:SvenssonBengt... | lld:pubmed |
| pubmed-article:18777103 | pubmed:author | pubmed-author:KollingDerric... | lld:pubmed |
| pubmed-article:18777103 | pubmed:author | pubmed-author:SeufferheldMa... | lld:pubmed |
| pubmed-article:18777103 | pubmed:author | pubmed-author:RoseStuartS | lld:pubmed |
| pubmed-article:18777103 | pubmed:author | pubmed-author:PaddenSeanS | lld:pubmed |
| pubmed-article:18777103 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18777103 | pubmed:volume | 98 | lld:pubmed |
| pubmed-article:18777103 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18777103 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18777103 | pubmed:pagination | 449-68 | lld:pubmed |
| pubmed-article:18777103 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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| pubmed-article:18777103 | pubmed:meshHeading | pubmed-meshheading:18777103... | lld:pubmed |
| pubmed-article:18777103 | pubmed:meshHeading | pubmed-meshheading:18777103... | lld:pubmed |
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| pubmed-article:18777103 | pubmed:meshHeading | pubmed-meshheading:18777103... | lld:pubmed |
| pubmed-article:18777103 | pubmed:articleTitle | D1-arginine257 mutants (R257E, K, and Q) of Chlamydomonas reinhardtii have a lowered QB redox potential: analysis of thermoluminescence and fluorescence measurements. | lld:pubmed |
| pubmed-article:18777103 | pubmed:affiliation | Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. | lld:pubmed |
| pubmed-article:18777103 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18777103 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:18777103 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18777103 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18777103 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:2716987 | entrezgene:pubmed | pubmed-article:18777103 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18777103 | lld:entrezgene |
