Post-translational amino acid conversion in photosystem II as a possible origin of photosynthetic oxygen evolution

Yuichiro Shimada, Takehiro Suzuki, Takumi Matsubara, Tomomi Kitajima-Ihara, Ryo Nagao, Naoshi Dohmae and Takumi Noguchi ()
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Yuichiro Shimada: Nagoya University, Furo-cho
Takehiro Suzuki: RIKEN Center for Sustainable Resource Science
Takumi Matsubara: Nagoya University, Furo-cho
Tomomi Kitajima-Ihara: Nagoya University, Furo-cho
Ryo Nagao: Nagoya University, Furo-cho
Naoshi Dohmae: RIKEN Center for Sustainable Resource Science
Takumi Noguchi: Nagoya University, Furo-cho

Nature Communications, 2022, vol. 13, issue 1, 1-8

Abstract: Abstract Photosynthetic oxygen evolution is performed at the Mn cluster in photosystem II (PSII). The advent of this reaction on ancient Earth changed its environment by generating an oxygenic atmosphere. However, how oxygen evolution originated during the PSII evolution remains unknown. Here, we characterize the site-directed mutants at the carboxylate ligands to the Mn cluster in cyanobacterial PSII. A His residue replaced for D1-D170 is found to be post-translationally converted to the original Asp to recover oxygen evolution. Gln/Asn residues in the mutants at D1-E189/D1-D342 are also converted to Glu/Asp, suggesting that amino-acid conversion is a common phenomenon at the ligand sites of the Mn cluster. We hypothesize that post-translational generation of carboxylate ligands in ancestral PSII could have led to the formation of a primitive form of the Mn cluster capable of partial water oxidation, which could have played a crucial role in the evolutionary process of photosynthetic oxygen evolution.

Date: 2022
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DOI: 10.1038/s41467-022-31931-y

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