Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 11, Issue 20, Pages 8908-8913Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.0c02411
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Funding
- Nanotechnology Platform Program Molecule and Material Synthesis of the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan [JPMXP0S20MS1007]
- JSPS KAKENHI [JP20H05096, JP17H06435, JP17H03662, JP17H06433]
- National Key R&D Program of China [2017YFA0503700]
- National Natural Science Foundation of China [31470339]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB17000000]
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The high-spin S-2 state was investigated with photosystem II (PSII) from spinach, Thermosynechococcus vulcanus, and Cyanidioschyzon merolae. In extrinsic protein-depleted PSII, high-spin electron paramagnetic resonance (EPR) signals were not detected in either species, whereas all species showed g similar to 5 signals in the presence of a high concentration of Ca2+ instead of the multiline signal. In the intact and PsbP/Qdepleted PSII from spinach, the g = 4.1 EPR signal was detected. These results show that formation of the high-spin S-2 state of the manganese cluster is regulated by the extrinsic proteins through a charge located near the Mn4 atom in the Mn4CaO5 cluster but is independent of the intrinsic proteins. The shift to the g similar to 5 state is caused by tilting of the z-axis in the Mn4 coordinates through hydrogen bonds or external divalent cations. The structural modification may allow insertion of an oxygen atom during the S-2-to-S-3 transition.
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