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PsbP-induced protein conformational changes around Cl ions in the water oxidizing center of photosystem II

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Photosynthetica

Abstract

PsbP is an extrinsic protein of PSII having a function of Ca2+ and Cl retention in the water-oxidizing center (WOC). In order to understand the mechanism how PsbP regulates the Cl binding in WOC, we examined the effect of PsbP depletion on the protein structures around the Cl sites using Fourier transform infrared (FTIR) spectroscopy. Light-induced FTIR difference spectra upon the S1→S2 transition were obtained using Cl-bound and NO3-substituted PSII membranes in the presence and absence of PsbP. A clear difference in the amide I band changes by PsbP depletion was observed between Cl-bound and NO3-substituted PSII samples, indicating that PsbP binding perturbed the protein conformations around the Clion(s) in WOC. It is suggested that PsbP stabilizes the Cl binding by regulating the dissociation constant of Cl and/or an energy barrier of Cl dissociation through protein conformational changes around the Cl ion(s).

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Abbreviations

DCMU:

3-(3,4-dichlorophenyl)-1,1-dimethylurea

FTIR:

Fourier transform infrared

Mes:

2-(N-morpholino) ethanesulfonic acid

PMS:

phenazine methosulfate

WOC:

water-oxidizing center

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Correspondence to T. Noguchi.

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Acknowledgments: This study was supported by the Grants-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology (17H03662 to T.N.).

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Kondo, J., Noguchi, T. PsbP-induced protein conformational changes around Cl ions in the water oxidizing center of photosystem II. Photosynthetica 56, 178–184 (2018). https://doi.org/10.1007/s11099-017-0749-5

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  • DOI: https://doi.org/10.1007/s11099-017-0749-5

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