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The 28 kDa apoprotein of CP 26 in PS II binds copper

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Abstract

Photosystem II (PS II) particles isolated from spinach in the presence of 10 μM CuSO4 contained 1.2 copper/300 Chl that was resistant to EDTA. When CuSO4 was not added during the isolation, PS II particles contained variable amounts of copper resistant to EDTA (0.1–1.1 copper/300 Chl). No correlation was found between copper content and oxygen evolving capacity of the PS II particles. To identify the copper binding protein, we developed a fractionation procedure which included solubilisation of PS II particles followed by precipitation with polyethylene glycol. A 22-fold purification of copper with respect to protein was achieved for a 28 kDa protein. Partial amino acid sequence of a 13 kDa fragment, obtained after V8 (endo Glu-C) protease treatment, showed identity with CP 26 over a 14 amino acid stretch. EPR measurements on the purified protein suggest oxygen and/or nitrogen as ligands for copper but tend to exclude sulfur. We conclude that the 28 kDa apoprotein of CP 26 from spinach binds one copper per molecule of CP 26. A possible function for this copper protein in the xanthophyll cycle is discussed.

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Abbreviations

CP 26 and CP 29:

chlorophyll a/b protein complex 26 and 29

LHC II:

light-harvesting chlorophyll a/b protein complex of Photosystem II

SB14:

sulfobetaine 14

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Arvidsson, PO., Bratt, C.E., Andréasson, LE. et al. The 28 kDa apoprotein of CP 26 in PS II binds copper. Photosynth Res 37, 217–225 (1993). https://doi.org/10.1007/BF00032825

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