Identification of a Na+-Binding Site near the Oxygen-Evolving Complex of Spinach Photosystem II

Jimin Wang; Joshua M. Perez-Cruet; Hao Li Huang; Krystle Reiss; Christopher J. Gisriel; Gourab Banerjee; Divya Kaur; Ipsita Ghosh; Alisha Dziarski; M. R. Gunner; Victor S. Batista; Gary W. Brudvig

doi:10.1021/acs.biochem.0c00303

Identification of a Na⁺-Binding Site near the Oxygen-Evolving Complex of Spinach Photosystem II

Jimin Wang, Joshua M. Perez-Cruet, Hao Li Huang, Krystle Reiss, Christopher J. Gisriel, Gourab Banerjee, Divya Kaur, Ipsita Ghosh, Alisha Dziarski, M. R. Gunner, Victor S. Batista, Gary W. Brudvig

Yale University

Research output: Contribution to journal › Article

Abstract

The oxygen-evolving complex (OEC) of photosystem II (PSII) is an oxomanganese cluster composed of four redox-active Mn ions and one redox-inactive Ca2+ ion, with two nearby bound Cl- ions. Sodium is a common counterion of both chloride and hydroxide anions, and a sodium-specific binding site has not been identified near the OEC. Here, we find that the oxygen-evolution activity of spinach PSII increases with Na+ concentration, particularly at high pH. A Na+-specific binding site next to the OEC, becomes available after deprotonation of the D1-H337 amino acid residue, is suggested by the analysis of two recently published PSII cryo-electron microscopy maps in combination with quantum mechanical calculations and multiconformation continuum electrostatics simulations.

Original language	English
Pages (from-to)	2823-2831
Number of pages	9
Journal	Biochemistry
Volume	59
Issue number	30
DOIs	https://doi.org/10.1021/acs.biochem.0c00303
Publication status	Published - Aug 4 2020

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1021/acs.biochem.0c00303

Fingerprint Dive into the research topics of 'Identification of a Na<sup>+</sup>-Binding Site near the Oxygen-Evolving Complex of Spinach Photosystem II'. Together they form a unique fingerprint.

Cite this

Wang, J., Perez-Cruet, J. M., Huang, H. L., Reiss, K., Gisriel, C. J., Banerjee, G., Kaur, D., Ghosh, I., Dziarski, A., Gunner, M. R., Batista, V. S., & Brudvig, G. W. (2020). Identification of a Na⁺-Binding Site near the Oxygen-Evolving Complex of Spinach Photosystem II. Biochemistry, 59(30), 2823-2831. https://doi.org/10.1021/acs.biochem.0c00303

Identification of a Na⁺-Binding Site near the Oxygen-Evolving Complex of Spinach Photosystem II. / Wang, Jimin; Perez-Cruet, Joshua M.; Huang, Hao Li; Reiss, Krystle; Gisriel, Christopher J.; Banerjee, Gourab; Kaur, Divya; Ghosh, Ipsita; Dziarski, Alisha; Gunner, M. R.; Batista, Victor S.; Brudvig, Gary W.

In: Biochemistry, Vol. 59, No. 30, 04.08.2020, p. 2823-2831.

Research output: Contribution to journal › Article

Wang, Jimin ; Perez-Cruet, Joshua M. ; Huang, Hao Li ; Reiss, Krystle ; Gisriel, Christopher J. ; Banerjee, Gourab ; Kaur, Divya ; Ghosh, Ipsita ; Dziarski, Alisha ; Gunner, M. R. ; Batista, Victor S. ; Brudvig, Gary W. / Identification of a Na⁺-Binding Site near the Oxygen-Evolving Complex of Spinach Photosystem II. In: Biochemistry. 2020 ; Vol. 59, No. 30. pp. 2823-2831.

@article{2e674c2bd08948be8f5e460868752978,

title = "Identification of a Na+-Binding Site near the Oxygen-Evolving Complex of Spinach Photosystem II",

abstract = "The oxygen-evolving complex (OEC) of photosystem II (PSII) is an oxomanganese cluster composed of four redox-active Mn ions and one redox-inactive Ca2+ ion, with two nearby bound Cl- ions. Sodium is a common counterion of both chloride and hydroxide anions, and a sodium-specific binding site has not been identified near the OEC. Here, we find that the oxygen-evolution activity of spinach PSII increases with Na+ concentration, particularly at high pH. A Na+-specific binding site next to the OEC, becomes available after deprotonation of the D1-H337 amino acid residue, is suggested by the analysis of two recently published PSII cryo-electron microscopy maps in combination with quantum mechanical calculations and multiconformation continuum electrostatics simulations. ",

author = "Jimin Wang and Perez-Cruet, {Joshua M.} and Huang, {Hao Li} and Krystle Reiss and Gisriel, {Christopher J.} and Gourab Banerjee and Divya Kaur and Ipsita Ghosh and Alisha Dziarski and Gunner, {M. R.} and Batista, {Victor S.} and Brudvig, {Gary W.}",

year = "2020",

month = aug,

day = "4",

doi = "10.1021/acs.biochem.0c00303",

language = "English",

volume = "59",

pages = "2823--2831",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "30",

}

TY - JOUR

T1 - Identification of a Na+-Binding Site near the Oxygen-Evolving Complex of Spinach Photosystem II

AU - Wang, Jimin

AU - Perez-Cruet, Joshua M.

AU - Huang, Hao Li

AU - Reiss, Krystle

AU - Gisriel, Christopher J.

AU - Banerjee, Gourab

AU - Kaur, Divya

AU - Ghosh, Ipsita

AU - Dziarski, Alisha

AU - Gunner, M. R.

AU - Batista, Victor S.

AU - Brudvig, Gary W.

PY - 2020/8/4

Y1 - 2020/8/4

N2 - The oxygen-evolving complex (OEC) of photosystem II (PSII) is an oxomanganese cluster composed of four redox-active Mn ions and one redox-inactive Ca2+ ion, with two nearby bound Cl- ions. Sodium is a common counterion of both chloride and hydroxide anions, and a sodium-specific binding site has not been identified near the OEC. Here, we find that the oxygen-evolution activity of spinach PSII increases with Na+ concentration, particularly at high pH. A Na+-specific binding site next to the OEC, becomes available after deprotonation of the D1-H337 amino acid residue, is suggested by the analysis of two recently published PSII cryo-electron microscopy maps in combination with quantum mechanical calculations and multiconformation continuum electrostatics simulations.

AB - The oxygen-evolving complex (OEC) of photosystem II (PSII) is an oxomanganese cluster composed of four redox-active Mn ions and one redox-inactive Ca2+ ion, with two nearby bound Cl- ions. Sodium is a common counterion of both chloride and hydroxide anions, and a sodium-specific binding site has not been identified near the OEC. Here, we find that the oxygen-evolution activity of spinach PSII increases with Na+ concentration, particularly at high pH. A Na+-specific binding site next to the OEC, becomes available after deprotonation of the D1-H337 amino acid residue, is suggested by the analysis of two recently published PSII cryo-electron microscopy maps in combination with quantum mechanical calculations and multiconformation continuum electrostatics simulations.

UR - http://www.scopus.com/inward/record.url?scp=85089616835&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85089616835&partnerID=8YFLogxK

U2 - 10.1021/acs.biochem.0c00303

DO - 10.1021/acs.biochem.0c00303

M3 - Article

C2 - 32650633

AN - SCOPUS:85089616835

VL - 59

SP - 2823

EP - 2831

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 30

ER -