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Bicarbonate activation of the monomeric photosystem II-PsbS/Psb27 complex

Fantuzzi, Andrea (author)
Department of Life Sciences, Imperial College London, London, United Kingdom
Haniewicz, Patrycja (author)
Department of Plant Physiology, Warsaw University of Life Sciences - SGGW, Warsaw, Poland; Laboratory of Structural Biology, International Institute of Molecular and Cell Biology, Warsaw, Poland
Farci, Domenica (author)
Umeå universitet,Kemiska institutionen
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Loi, M Cecilia (author)
Department of Life and Environmental Sciences, University of Cagliari, Cagliari, Italy
Park, Keunha (author)
Department of Life Sciences, Imperial College London, London, United Kingdom
Büchel, Claudia (author)
Institute of Molecular Biosciences, University of Frankfurt, Frankfurt am Main, Germany
Bochtler, Matthias (author)
Laboratory of Structural Biology, International Institute of Molecular and Cell Biology, Warsaw, Poland; Polish Academy of Science, Institute of Biochemistry and Biophysics, Warsaw, Poland
Rutherford, A William (author)
Department of Life Sciences, Imperial College London, London, United Kingdom
Piano, Dario (author)
Laboratory of Structural Biology, International Institute of Molecular and Cell Biology, Warsaw, Poland; Department of Life and Environmental Sciences, University of Cagliari, Cagliari, Italy
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 (creator_code:org_t)
Oxford University Press, 2023
2023
English.
In: Plant Physiology. - : Oxford University Press. - 0032-0889 .- 1532-2548. ; 192:4, s. 2656-2671
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • In thylakoid membranes, photosystem II (PSII) monomers from the stromal lamellae contain the subunits PsbS and Psb27 (PSIIm-S/27), while PSII monomers (PSIIm) from granal regions lack these subunits. Here, we have isolated and characterized these 2 types of PSII complexes in tobacco (Nicotiana tabacum). PSIIm-S/27 showed enhanced fluorescence, the near absence of oxygen evolution, and limited and slow electron transfer from QA to QB compared to the near-normal activities in the granal PSIIm. However, when bicarbonate was added to PSIIm-S/27, water splitting and QA to QB electron transfer rates were comparable to those in granal PSIIm. The findings suggest that the binding of PsbS and/or Psb27 inhibits forward electron transfer and lowers the binding affinity for bicarbonate. This can be rationalized in terms of the recently discovered photoprotection role played by bicarbonate binding via the redox tuning of the QA/QA•- couple, which controls the charge recombination route, and this limits chlorophyll triplet-mediated 1O2 formation. These findings suggest that PSIIm-S/27 is an intermediate in the assembly of PSII in which PsbS and/or Psb27 restrict PSII activity while in transit using a bicarbonate-mediated switch and protective mechanism.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

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