In Tris-washed chloroplasts the kinetics of the primary electron acceptor X 320 of reaction center II has been investigated by fast repetitive flash spectroscopy with a time resolution of approximately 1 mus. It has been found that X 320 is reduced by a flash in less than or equal to 1 mus. The subsequent reoxidation in the dark occurs mainly by a reaction with a 100-200 mus kinetics. The light-induced difference spectrum confirms X 320 to be the reactive species. From these results it is concluded that in Tris-washed chloroplasts the reaction centers of System II are characterized by a high photochemical turnover rate mediated either via rapid direct charge recombination or via fast cyclic electron flow.
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http://dx.doi.org/10.1016/0005-2728(76)90214-0 | DOI Listing |
Arch Biochem Biophys
May 2008
Departamento de Estrés Abiótico, Instituto de Recursos Naturales y Agrobiología de Salamanca (IRNASA-CSIC), Apdo. 257, 37071 Salamanca, Spain.
Peroxynitrite is a strong oxidant that has been proposed to form in chloroplasts. The interaction between peroxynitrite and photosystem II (PSII) has been investigated to determine whether this oxidant could be a hazard for PSII. Peroxynitrite is shown to inhibit oxygen evolution in PSII membranes in a dose-dependent manner.
View Article and Find Full Text PDFBiochim Biophys Acta
April 2008
Wageningen University, Laboratory of Biophysics, PO Box 8128, 6700 ET Wageningen, The Netherlands.
Non-bilayer lipids account for about half of the total lipid content in chloroplast thylakoid membranes. This lends high propensity of the thylakoid lipid mixture to participate in different phases which might be functionally required. It is for instance known that the chloroplast enzyme violaxanthin de-epoxidase (VDE) requires a non-bilayer phase for proper functioning in vitro but direct evidence for the presence of non-bilayer lipid structures in thylakoid membranes under physiological conditions is still missing.
View Article and Find Full Text PDFBiochim Biophys Acta
February 2002
Department of Biophysics, Huygens Laboratory, Leiden University, P.O. Box 9504, 2300 RA, Leiden, The Netherlands.
Loss by recombination of the charge separated state P(680+)Q(A-) limits the performance of Photosystem II (PS II) as a photochemical energy converter. Time constants reported in literature for this process are mostly either near 0.17 ms or near 1.
View Article and Find Full Text PDFBiochemistry
August 1994
Department of Biology, University College London, U.K.
Electron nuclear double resonance (ENDOR) and special triple (ST) resonance spectroscopies have been used to study the cation radicals of the primary donor, P680, and two secondary donor chlorophylls (Chl) in photosystem 2 (PS2). Two different preparations were employed, Tris-washed PS2 membranes and PS2 reaction centers (D1-D2-I-Cytb559 complex). One secondary donor Chl a cation radical, Chl1.
View Article and Find Full Text PDFFEBS Lett
March 1991
Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, Sweden.
The D1 reaction center protein in photosystem II is rapidly degraded during illumination of chloride-depleted or Tris-washed thylakoids. The degradation is independent of oxygen and occurs under anaerobic conditions provided that electrons can flow through the acceptor-side of photosystem II. This shows that oxygen-derived reactive species are not necessarily involved in the light-dependent damage of the D1 protein.
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