Redesign of the <i>Chlamydomonas reinhardtii</i><scp>Q<sub>B</sub></scp> binding niche reveals photosynthesis works in the absence of a driving force for <scp>Q<sub>A</sub></scp>‐<scp>Q<sub>B</sub></scp> electron transfer

An in silico redesign of the secondary quinone electron acceptor (Q<sub>B</sub>) 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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Publication Details

Journal
Physiologia Plantarum
Published
2024-11-01
DOI
https://doi.org/10.1111/ppl.70008
Citations
1
Primary Topic
Photosynthetic Processes and Mechanisms
Type
article
Field-Weighted Citation Impact
0.23

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article

Redesign of the Chlamydomonas reinhardtiiQB binding niche reveals photosynthesis works in the absence of a driving force for QA‐QB electron transfer

Violeta Peeva, Taras К. Antal, Maria Teresa Giardi, Ivo Bertalan et al.
1 citations
Physiologia Plantarum
Photosynthetic Processes and Mechanisms
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Redesign of the Chlamydomonas reinhardtiiQB binding niche reveals photosynthesis works in the absence of a driving force for QA‐QB electron transfer

Violeta Peeva, Taras К. Antal, Maria Teresa Giardi, Ivo Bertalan, Veranika Zobnina, Udo Johanningmeier, Manju Ray, Paula Mulo, Olli Virtanen, Maya D. Lambreva, Esa Tyystjärvi, Fabio Polticelli, Giuseppina Rea
article en
1 citations

Abstract

An in silico redesign of the secondary quinone electron acceptor (Q<sub>B</sub>) 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.

Physiologia PlantarumVol. 176(6)
Roma Tre University (IT), University of Turku (FI), Bulgarian Academy of Sciences (BG), Biosensor (Italy) (IT), Institute of Plant Physiology and Genetics (BG), Pskov State University (RU), National Research Council (IT), Institute of Crystallography (IT), Institute for Biological Systems, Martin Luther University Halle-Wittenberg (DE), Vrije Universiteit Amsterdam (NL)
European Cooperation in Science and Technology, Academy of Finland, Novo Nordisk, Novo Nordisk Fonden, Regione Lazio
Openalex Percentile: Top 40%
Photosynthetic Processes and Mechanisms
0.23
DOIOpen Access PDFOpenAlex
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