EPR/ENDOR characterization of the physical and electronic structure of the OEC Mn cluster

• Published in: BBA - Bioenergetics Vol. 1503; no. 1; pp. 96 - 111
• Main Authors: Peloquin, Jeffrey M., Britt, R.David
• Format: Book Review Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 05.01.2001
• Subjects: Electron nuclear double resonance; Electron paramagnetic resonance; Electron Spin Resonance Spectroscopy; Manganese; Manganese - chemistry; Models, Molecular; Oxygen - chemistry; Oxygen evolution; Photosynthesis; Photosynthetic Reaction Center Complex Proteins - chemistry; Photosystem II; Photosystem II Protein Complex; Oxygen evolution; Photosystem II; Electron paramagnetic resonance; Photosynthesis; Electron nuclear double resonance; Manganese
• ISSN: 0005-2728; 0006-3002; 1879-2650
• DOI: 10.1016/S0005-2728(00)00219-X

Electron paramagnetic resonance (EPR) spectroscopy has often played a crucial role in characterizing the various cofactors and processes of photosynthesis, and photosystem II and its oxygen evolving chemistry is no exception. Until recently, the application of EPR spectroscopy to the characterization of the oxygen evolving complex (OEC) has been limited to the S 2-state of the Kok cycle. However, in the past few years, continuous wave-EPR signals have been obtained for both the S 0- and S 1-state as well as for the S 2–Y Z-state of a number of inhibited systems. Furthermore, the pulsed EPR technique of electron spin echo electron nuclear double resonance spectroscopy has been used to directly probe the 55Mn nuclei of the manganese cluster. In this review, we discuss how the EPR data obtained from each of these states of the OEC Kok cycle are being used to provide insight into the physical and electronic structure of the manganese cluster and its interaction with the key tyrosine, Y Z.