Evidence for direct interaction between the chlorophyll-proteins CP29 and CP47 in photosystem II.
Fractionation by anionic-exchange chromatography of an oxygen-evolving photosystem II complex solubilized with 10 mM dodecyl maltoside shows the existence of a sovra-molecular complex between the internal chlorophyll a antenna CP47 and the chlorophyll a/b minor antenna CP29. The chromatographic result is confirmed by a cross-linking experiment which brings about a binary conjugate formed by CP47 and CP29. The sovra-molecular complex between the two chlorophyll protein-complexes has a low temperature fluorescence emission red shifted with respect to the two isolated antenna components. A possible two arms antenna topology for photosystem II is suggested.
Rigoni
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Dipartimento di Biologia, Università di Padova, Italy.
Barbato
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R
Friso
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Giacometti
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GM
D001059:Apoproteins / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes; D008970:Molecular Weight; D045322:Photosynthetic Reaction Center Complex Proteins / Q000302:isolation & purification / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D013050:Spectrometry, Fluorescence
D001059:Apoproteins; C069660:CP29 light harvesting complex; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex