Literature DB >> 17320041

Insights into the function of PsbR protein in Arabidopsis thaliana.

Yagut Allahverdiyeva1, Fikret Mamedov, Marjaana Suorsa, Stenbjörn Styring, Imre Vass, Eva-Mari Aro.   

Abstract

The functional state of the Photosystem (PS) II complex in Arabidopsis psbR T-DNA insertion mutant was studied. The DeltaPsbR thylakoids showed about 34% less oxygen evolution than WT, which correlates with the amounts of PSII estimated from Y(D)(ox) radical EPR signal. The increased time constant of the slow phase of flash fluorescence (FF)-relaxation and upshift in the peak position of the main TL-bands, both in the presence and in the absence of DCMU, confirmed that the S(2)Q(A)(-) and S(2)Q(B)(-) charge recombinations were stabilized in DeltaPsbR thylakoids. Furthermore, the higher amount of dark oxidized Cyt-b559 and the increased proportion of fluorescence, which did not decay during the 100s time span of the measurement thus indicating higher amount of Y(D)(+)Q(A)(-) recombination, pointed to the donor side modifications in DeltaPsbR. EPR measurements revealed that S(1)-to-S(2)-transition and S(2)-state multiline signal were not affected by mutation. The fast phase of the FF-relaxation in the absence of DCMU was significantly slowed down with concomitant decrease in the relative amplitude of this phase, indicating a modification in Q(A) to Q(B) electron transfer in DeltaPsbR thylakoids. It is concluded that the lack of the PsbR protein modifies both the donor and the acceptor side of the PSII complex.

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Year:  2007        PMID: 17320041     DOI: 10.1016/j.bbabio.2007.01.011

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  15 in total

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9.  Spring Ephemerals Adapt to Extremely High Light Conditions via an Unusual Stabilization of Photosystem II.

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Review 10.  Structure and Function of the Photosystem Supercomplexes.

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Journal:  Front Plant Sci       Date:  2018-03-20       Impact factor: 5.753

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