D139N mutation of PsbP enhances the oxygen-evolving activity of photosystem II through stabilized binding of a chloride ion.

ABSTRACT: Photosystem II (PSII) is a multisubunit membrane protein complex that catalyzes light-driven oxidation of water to molecular oxygen. The chloride ion (Cl^-) has long been known as an essential cofactor for oxygen evolution by PSII, and two Cl^- ions (Cl-1 and Cl-2) have been found to specifically bind near the Mn₄CaO₅ cluster within the oxygen-evolving center (OEC). However, despite intensive studies on these Cl^- ions, little is known about the function of Cl-2, the Cl^- ion that is associated with the backbone nitrogens of D1-Asn338, D1-Phe339, and CP43-Glu354. In green plant PSII, the membrane extrinsic subunits-PsbP and PsbQ-are responsible for Cl^- retention within the OEC. The Loop 4 region of PsbP, consisting of

SUBMITTER: Imaizumi K 

PROVIDER: S-EPMC9896922 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature