A1 Refereed original research article in a scientific journal
Redesign of the Chlamydomonas reinhardtii QB binding niche reveals photosynthesis works in the absence of a driving force for QA‐QB electron transfer
Authors: Lambreva, Maya D.; Zobnina, Veranika; Antal, Taras K.; Peeva, Violeta N.; Giardi, Maria Teresa; Bertalan, Ivo; Johanningmeier, Udo; Virtanen, Olli; Ray, Mithila; Mulo, Paula; Polticelli, Fabio; Tyystjärvi, Esa; Rea, Giuseppina
Publisher: Wiley
Publication year: 2024
Journal: Physiologia Plantarum
Journal name in source: Physiologia Plantarum
Article number: e70008
Volume: 176
Issue: 6
ISSN: 0031-9317
eISSN: 1399-3054
DOI: https://doi.org/10.1111/ppl.70008
Web address : https://doi.org/10.1111/ppl.70008
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/478046305
An in silico redesign of the secondary quinone electron acceptor (QB) binding pocket of the D1 protein of Photosystem II (PSII) suggested that mutations of the F265 residue would affect atrazine binding. Chlamydomonas reinhardtii mutants F265T and F265S were produced to obtain atrazine-hypersensitive strains for biosensor applications, and the mutants were indeed found to be more atrazine-sensitive than the reference strain IL. Fluorescence and thermoluminescence data agree with a weak driving force and confirm slow electron transfer but cannot exclude an additional effect on protonation of the secondary quinone. Both mutants grow autotrophically, indicating that PSII requires strong light for optimal function, as was the case in the ancestral homodimeric reaction center.
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Funding information in the publication:
Regione Lazio, Grant n. 85-2017-15256; European Cooperation in Science and Technology, COST Action TD1102; Novo Nordisk Fonden, grant NNF220C0079284, Academy of Finland, grant 333421, CNR project FOE-2021, grant dba.ad005.225
