Abstract
Photosystem II (PSII) is a photosynthetic membrane-protein complex that undergoes an intricate, tightly regulated cycle of assembly, damage, and repair. The available crystal structures of cyanobacterial PSII are an essential foundation for understanding PSII function, but nonetheless provide a snapshot only of the active complex. To study aspects of the entire PSII life-cycle, mass spectrometry (MS) has emerged as a powerful tool that can be used in conjunction with biochemical techniques. In this article, we present the MS-based approaches that are used to study PSII composition, dynamics, and structure, and review the information about the PSII life-cycle that has been gained by these methods. This information includes the composition of PSII subcomplexes, discovery of accessory PSII proteins, identification of post-translational modifications and quantification of their changes under various conditions, determination of the binding site of proteins not observed in PSII crystal structures, conformational changes that underlie PSII functions, and identification of water and oxygen channels within PSII. We conclude with an outlook for the opportunity of future MS contributions to PSII research.
Highlights
Since the late 1990s, mass spectrometry (MS) has become a central tool for the study of proteins and their role in biology
Scarcity of genomic sequence data combined with low instrument sensitivity, mass accuracy, and fragmentation efficiency meant that sample analysis was mainly restricted to highly purified Photosystem II (PSII) complexes or individual subunits, with poor capability for novel protein identification
The use of MS has been fueled by improvements in sample preparation methods for analysis of membrane proteins, increasing availability of MS instrumentation, and significant advances in instrument sensitivity, speed, and mass accuracy
Summary
Since the late 1990s, mass spectrometry (MS) has become a central tool for the study of proteins and their role in biology. Scarcity of genomic sequence data combined with low instrument sensitivity, mass accuracy, and fragmentation efficiency meant that sample analysis was mainly restricted to highly purified PSII complexes or individual subunits, with poor capability for novel protein identification.
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