TY - JOUR
T1 - Formation of the High-Spin S2State Related to the Extrinsic Proteins in the Oxygen Evolving Complex of Photosystem II
AU - Taguchi, Shota
AU - Shen, Liangliang
AU - Han, Guangye
AU - Umena, Yasufumi
AU - Shen, Jian Ren
AU - Noguchi, Takumi
AU - Mino, Hiroyuki
N1 - Funding Information:
This work was partly supported by a Nanotechnology Platform Program “Molecule and Material Synthesis” (JPMXP0S20MS1007) of the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan (to H.M); JSPS KAKENHI Grant JP20H05096 (to H.M.); Grants JP17H06435, JP17H03662, and JP17H06433 (to T.N.); and the National Key R&D Program of China (2017YFA0503700), the National Natural Science Foundation of China (31470339), a Strategic Priority Research Program of the Chinese Academy of Sciences (XDB17000000).
Publisher Copyright:
© 2020 American Chemical Society.
PY - 2020/10/15
Y1 - 2020/10/15
N2 - The high-spin S2 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 ∼5 signals in the presence of a high concentration of Ca2+ instead of the multiline signal. In the intact and PsbP/Q-depleted PSII from spinach, the g = 4.1 EPR signal was detected. These results show that formation of the high-spin S2 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 ∼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 S2-to-S3 transition.
AB - The high-spin S2 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 ∼5 signals in the presence of a high concentration of Ca2+ instead of the multiline signal. In the intact and PsbP/Q-depleted PSII from spinach, the g = 4.1 EPR signal was detected. These results show that formation of the high-spin S2 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 ∼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 S2-to-S3 transition.
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U2 - 10.1021/acs.jpclett.0c02411
DO - 10.1021/acs.jpclett.0c02411
M3 - Article
C2 - 32990440
AN - SCOPUS:85093538893
VL - 11
SP - 8908
EP - 8913
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
SN - 1948-7185
IS - 20
ER -