Structural analysis of extrinsic PsbP protein of PSII from Spinacea oleracea and its interaction with the oxygen-evolving complex

0341146 - ÚVGZ 2011 US eng A - Abstract
Kohoutová, Jaroslava - Kopecký, V. - Lapkouski, Mikalai - Hofbauerová, Kateřina - Sovová, Žofie - Gonzáles-Perezc, S. - Smatanová, I.K. - Revuelta, J. L. - Arellano, J.B. - Ettrich, Rüdiger
Structural analysis of extrinsic PsbP protein of PSII from Spinacea oleracea and its interaction with the oxygen-evolving complex.
FEBS Journal. Roč. 1, č. 276 (2009), s. 146-147. ISSN 1742-464X. E-ISSN 1742-4658.
[Congress of the Federation-of-European-Biochemical-Societies /34./. 04.07.2009-09.07.2009, Prague]
Institutional research plan: CEZ:AV0Z60870520; CEZ:AV0Z50200510
Keywords : protein
Subject RIV: CE - Biochemistry

Photosynthesis is the process by which the light energy is converted into the chemical energy. It takes place in the thylakoid membrane of higher plants, algae and cyanobacteria, where membrane-embedded, pigment-protein PSII complex performs light-driven oxidation of water with concomitant reduction of the plastoquinone pool. Water splitting is performed in a cluster of four Mn2+ ions located on the lumenal side of photosystem II (PSII) and Ca2+ and Cl- ions are required for optimal activity of this water–oxidase complex. In higher plants the function of Ca2+ and Cl- is modulated by the presence of four extrinsic proteins [1], PsbP, PsbQ [2], PsbO, and PsbR, at the lumenal surface, the so called oxygen-evolving complex. To understand the molecular mechanisms of the oxygen–evolving reaction, an essential prerequisite is the structural knowledge of these proteins and their relative interactions.
Permanent Link: http://hdl.handle.net/11104/0184223