Structural Dynamics of a Protein Domain Relevant to the Water-Oxidizing Complex in Photosystem II as Visualized by High-Speed Atomic Force Microscopy

• Published in: The journal of physical chemistry. B Vol. 124; no. 28; pp. 5847 - 5857
• Main Authors: Tokano, Takaya, Kato, Yuki, Sugiyama, Shogo, Uchihashi, Takayuki, Noguchi, Takumi
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 16.07.2020
• Subjects: B: Biophysics; Physical Chemistry of Biological Systems and Biomolecules; Microscopy, Atomic Force; Oxidation-Reduction; Photosystem II Protein Complex - metabolism; Protein Domains; Water
• ISSN: 1520-6106; 1520-5207
• DOI: 10.1021/acs.jpcb.0c03892

Photosystem II (PSII) is a multiprotein complex that has a function of light-driven water oxidation. The catalytic site of water oxidation is the Mn4CaO5 cluster, which is bound to the lumenal side of PSII through amino acid residues from the D1 and CP43 proteins and is further surrounded by the extrinsic proteins. In this study, we have for the first time visualized the structural dynamics of the lumenal region of a PSII core complex using high-speed atomic force microscopy (HS-AFM). The HS-AFM images of a PSII membrane fragment showed stepwise dissociation of the PsbP and PsbO extrinsic proteins. Upon subsequent destruction of the Mn4CaO5 cluster, the lumenal domain of CP43 was found to undergo a conformational fluctuation. The observed structural flexibility and conformational fluctuation of the CP43 lumenal domain are suggested to play important roles in the biogenesis of PSII and the photoassembly of the Mn4CaO5 cluster.