TY - JOUR
T1 - Post-translational amino acid conversion in photosystem II as a possible origin of photosynthetic oxygen evolution
AU - Shimada, Yuichiro
AU - Suzuki, Takehiro
AU - Matsubara, Takumi
AU - Kitajima-Ihara, Tomomi
AU - Nagao, Ryo
AU - Dohmae, Naoshi
AU - Noguchi, Takumi
N1 - Funding Information:
We thank Drs. Johannes Messinger, Tanai Cardona, Peter J. Nixon, and Nicholas Cox for valuable discussions. The computation was performed using Research Center for Computational Science, Okazaki, Japan (Project: 22-OMS-C084, 21-IMS-C082). This study was supported by JSPS KAKENHI Grant Number JP17H06433 and JP17H06435 (to T.N.).
Publisher Copyright:
© 2022, The Author(s).
PY - 2022/12
Y1 - 2022/12
N2 - 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.
AB - 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.
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U2 - 10.1038/s41467-022-31931-y
DO - 10.1038/s41467-022-31931-y
M3 - Article
C2 - 35864123
AN - SCOPUS:85134504154
SN - 2041-1723
VL - 13
JO - Nature communications
JF - Nature communications
IS - 1
M1 - 4211
ER -