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Bicarbonate activation of the monomeric photosystem II-PsbS/Psb27 complex.
Fantuzzi, Andrea; Haniewicz, Patrycja; Farci, Domenica; Loi, M Cecilia; Park, Keunha; Büchel, Claudia; Bochtler, Matthias; Rutherford, A William; Piano, Dario.
Afiliação
  • Fantuzzi A; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
  • Haniewicz P; Department of Plant Physiology, Warsaw University of Life Sciences - SGGW, Warsaw 02-776, Poland.
  • Farci D; Laboratory of Structural Biology, International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.
  • Loi MC; Department of Chemistry, Umea University, 90187 Umea, Sweden.
  • Park K; Department of Life and Environmental Sciences, University of Cagliari, Cagliari 09123, Italy.
  • Büchel C; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.
  • Bochtler M; Institute of Molecular Biosciences, University of Frankfurt, Frankfurt am Main 60438, Germany.
  • Rutherford AW; Laboratory of Structural Biology, International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.
  • Piano D; Polish Academy of Science, Institute of Biochemistry and Biophysics, Warsaw 02-106, Poland.
Plant Physiol ; 192(4): 2656-2671, 2023 08 03.
Article em En | MEDLINE | ID: mdl-37202365
ABSTRACT
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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bicarbonatos / Complexo de Proteína do Fotossistema II Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bicarbonatos / Complexo de Proteína do Fotossistema II Idioma: En Ano de publicação: 2023 Tipo de documento: Article