TY - JOUR
T1 - PH-Dependent Regulation of Electron Flow in Photosystem II by a Histidine Residue at the Stromal Surface
AU - Kobayashi, Tomoyuki
AU - Shimada, Yuichiro
AU - Nagao, Ryo
AU - Noguchi, Takumi
N1 - Funding Information:
This study was supported by JSPS KAKENHI Grant Number JP17H06435 and JP17H06433 (to T.N.).
Publisher Copyright:
©
PY - 2022
Y1 - 2022
N2 - In photosystem II (PSII), the secondary plastoquinone electron acceptor QB functions as a substrate that converts into plastoquinol upon its double reduction by electrons abstracted from water. It has been suggested that a histidine residue, D1-H252, which is located at the stromal surface near QB, is involved in the pH-dependent regulation of electron flow and proton transfer to QB. However, definitive evidence for the involvement of D1-H252 in the QB reactions has not been obtained yet. Here, we studied the roles of D1-H252 in PSII using a cyanobacterial mutant, in which D1-H252 was replaced with Ala. Delayed luminescence (DL) measurement upon a single flash showed a faster QB- decay at higher pH in the thylakoids from the wild-type strain due to the downshift of the redox potential of QB [Em(QB-/QB)]. This pH dependence of the QB- decay was lost in the D1-H252A mutant. The experimental Em(QB-/QB) changes were well reproduced by the density functional theory calculations for models with different protonation states of D1-H252 and with Ala replaced for H252. It was further shown that the period-four oscillation of the DL intensity by successive flashes was significantly diminished in the D1-H252A mutant, suggesting the inhibition of plastoquinone exchange at the QB pocket in this mutant. It is thus concluded that D1-H252 is a key amino acid residue that regulates electron flow in PSII by sensing pH in the stroma and stabilizes the QB binding site to facilitate the quinone exchange reaction.
AB - In photosystem II (PSII), the secondary plastoquinone electron acceptor QB functions as a substrate that converts into plastoquinol upon its double reduction by electrons abstracted from water. It has been suggested that a histidine residue, D1-H252, which is located at the stromal surface near QB, is involved in the pH-dependent regulation of electron flow and proton transfer to QB. However, definitive evidence for the involvement of D1-H252 in the QB reactions has not been obtained yet. Here, we studied the roles of D1-H252 in PSII using a cyanobacterial mutant, in which D1-H252 was replaced with Ala. Delayed luminescence (DL) measurement upon a single flash showed a faster QB- decay at higher pH in the thylakoids from the wild-type strain due to the downshift of the redox potential of QB [Em(QB-/QB)]. This pH dependence of the QB- decay was lost in the D1-H252A mutant. The experimental Em(QB-/QB) changes were well reproduced by the density functional theory calculations for models with different protonation states of D1-H252 and with Ala replaced for H252. It was further shown that the period-four oscillation of the DL intensity by successive flashes was significantly diminished in the D1-H252A mutant, suggesting the inhibition of plastoquinone exchange at the QB pocket in this mutant. It is thus concluded that D1-H252 is a key amino acid residue that regulates electron flow in PSII by sensing pH in the stroma and stabilizes the QB binding site to facilitate the quinone exchange reaction.
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U2 - 10.1021/acs.biochem.2c00150
DO - 10.1021/acs.biochem.2c00150
M3 - Article
C2 - 35686693
AN - SCOPUS:85133516483
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
ER -