Structure Function Studies of Photosystem II Using X-Ray Free Electron Lasers

• Published in: Annual review of biophysics Vol. 53; no. 1; pp. 343 - 365
• Main Authors: Yano, Junko, Kern, Jan, Yachandra, Vittal K
• Format: Journal Article
• Language: English
• Published: United States Annual Reviews 16.07.2024
• Subjects: Electrons; Lasers; manganese; Models, Molecular; Oxidation-Reduction; oxygen-evolving complex; photosynthetic water oxidation; photosystem II; Photosystem II Protein Complex - chemistry; Photosystem II Protein Complex - metabolism; Photosystem II Protein Complex - ultrastructure; Water - chemistry; Water - metabolism; X-ray crystallography; X-ray free electron laser; X-Rays; X-ray crystallography; photosystem II; photosynthetic water oxidation; oxygen-evolving complex; X-ray free electron laser; manganese
• ISSN: 1936-122X; 1936-1238
• DOI: 10.1146/annurev-biophys-071723-102519

The structure and mechanism of the water-oxidation chemistry that occurs in photosystem II have been subjects of great interest. The advent of X-ray free electron lasers allowed the determination of structures of the stable intermediate states and of steps in the transitions between these intermediate states, bringing a new perspective to this field. The room-temperature structures collected as the photosynthetic water oxidation reaction proceeds in real time have provided important novel insights into the structural changes and the mechanism of the water oxidation reaction. The time-resolved measurements have also given us a view of how this reaction—which involves multielectron, multiproton processes—is facilitated by the interaction of the ligands and the protein residues in the oxygen-evolving complex. These structures have also provided a picture of the dynamics occurring in the channels within photosystem II that are involved in the transport of the substrate water to the catalytic center and protons to the bulk.