Recent advances in the use of mass spectrometry to examine structure/function relationships in photosystem II

• Published in: Journal of photochemistry and photobiology. B, Biology Vol. 152; no. Pt B; pp. 227 - 246
• Main Authors: Bricker, Terry M., Mummadisetti, Manjula P., Frankel, Laurie K.
• Format: Journal Article
• Language: English
• Published: Switzerland Elsevier B.V 01-11-2015; Elsevier
• Subjects: Chemical protein modification; Chlorophyta - enzymology; Cyanobacteria - enzymology; Mass Spectrometry - methods; Membrane proteins; Photosynthesis; Photosystem II; Photosystem II Protein Complex - chemistry; Photosystem II Protein Complex - metabolism; Protein–protein interactions; Structure-Activity Relationship; Tandem mass spectrometry; Chemical protein modification; Tandem mass spectrometry; Photosystem II; Protein–protein interactions; Photosynthesis; Membrane proteins
• ISSN: 1011-1344; 1873-2682
• DOI: 10.1016/j.jphotobiol.2015.08.031

•Recent use of mass spectrometry in examining PS II structure/function is reviewed.•Background on PS II, mass spectrometry and protein modification is presented.•Future directions for the use of these techniques in PS II are discussed.
Tandem mass spectrometry often coupled with chemical modification techniques, is developing into increasingly important tool in structural biology. These methods can provide important supplementary information concerning the structural organization and subunit make-up of membrane protein complexes, identification of conformational changes occurring during enzymatic reactions, identification of the location of posttranslational modifications, and elucidation of the structure of assembly and repair complexes. In this review, we will present a brief introduction to Photosystem II, tandem mass spectrometry and protein modification techniques that have been used to examine the photosystem. We will then discuss a number of recent case studies that have used these techniques to address open questions concerning PS II. These include the nature of subunit–subunit interactions within the phycobilisome, the interaction of phycobilisomes with Photosystem I and the Orange Carotenoid Protein, the location of CyanoQ, PsbQ and PsbP within Photosystem II, and the identification of phosphorylation and oxidative modification sites within the photosystem. Finally, we will discuss some of the future prospects for the use of these methods in examining other open questions in PS II structural biochemistry.