Purification and characterization of oxygen-evolving photosystem II core complexes from the green alga Chlamydomonas reinhardtii.
Oxygen-evolving photosystem II complexes were isolated from the green alga Chlamydomonas reinhardtii by selective solubilization of thylakoid membranes with dodecyl maltoside followed by density gradient centrifugation and anion-exchange chromatography. In the presence of CaCl2 and K3[Fe(CN)6] the complexes evolved oxygen at rates exceeding 1000 mumol (mg of chl)-1 h-1. The particles contained 40 chlorophylls a and had properties very similar to those of PSII isolated from higher plants. Chlamydomonas reinhardtii is now the first organism which can be used for both site-directed mutagenesis and detailed biochemical and biophysical characterization of oxygen-evolving photosystem II. It seems therefore to be an ideal model organism for investigation of structure-function relationships in photosynthetic oxygen evolution.
Bumann
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Department of Membrane Biochemistry, Max Planck Institute for Biochemistry, Martinsried, Germany.
Oesterhelt
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D000818:Animals; D016825:Chlamydomonas reinhardtii / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D010100:Oxygen / Q000378:metabolism*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000302:isolation & purification* / Q000378:metabolism; D045332:Photosystem II Protein Complex
D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010100:Oxygen