Abstract
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.
Original language | English |
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Article number | e70008 |
Pages (from-to) | 1-16 |
Number of pages | 16 |
Journal | Physiologia Plantarum |
Volume | 176 |
Issue number | 6 |
Early online date | 14 Dec 2024 |
DOIs | |
Publication status | Published - Dec 2024 |
Bibliographical note
Publisher Copyright:© 2024 The Author(s). Physiologia Plantarum published by John Wiley & Sons Ltd on behalf of Scandinavian Plant Physiology Society.