Identification of Oxidized Amino Acid Residues in the Vicinity of the Mn4CaO5 Cluster of Photosystem II: Implications for the Identification of Oxygen Channels within the Photosystem

As a light-driven water–plastoquinone oxidoreductase, Photosystem II produces molecular oxygen as an enzymatic product. Additionally, under a variety of stress conditions, reactive oxygen species are produced at or near the active site for oxygen evolution. In this study, Fourier-transform ion cyclo...

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Bibliographic Details
Published in:Biochemistry (Easton) 2012-08, Vol.51 (32), p.6371-6377
Main Authors: Frankel, Laurie K, Sallans, Larry, Limbach, Patrick A, Bricker, Terry M
Format: Article
Language:English
Online Access:Get full text
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Summary:As a light-driven water–plastoquinone oxidoreductase, Photosystem II produces molecular oxygen as an enzymatic product. Additionally, under a variety of stress conditions, reactive oxygen species are produced at or near the active site for oxygen evolution. In this study, Fourier-transform ion cyclotron resonance mass spectrometry was used to identify oxidized amino acid residues located in several core Photosystem II proteins (D1, D2, CP43, and CP47) isolated from spinach Photosystem II membranes. While the majority of these oxidized residues (81%) are located on the oxygenated solvent-exposed surface of the complex, several residues on the CP43 protein (354E, 355T, 356M, and 357R) which are in close proximity (
ISSN:0006-2960
1520-4995
DOI:10.1021/bi300650n