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Ca2+ and Mg2+-binding and a putative calmodulin type Ca2+-binding site in Synechococcus Photosystem II

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Abstract

Thylakoids and Photosystem II particles prepared from the cyanobacterium Synechococcus PCC 7942 washed with a HEPES/glycerol buffer exhibited low rates of light-induced oxygen evolution. Addition of either Ca2+ or Mg2+ to both thylakoids and Photosystem II particles increased oxygen evolution independently, maximal rates being obtained by addition of both ions. If either preparation was washed with NaCl, light induced O2 evolution was completely inhibited, but re-activated in the same manner by Ca2+ and Mg2+ but to a lower level. In the presence of Mg2+, the reactivation of O2 evolution by Ca2+ allowed sigmoid kinetics, implying co-operative binding. The results are interpreted as indicating that not only Ca2+, but also Mg2+, is essential for light-induced oxygen evolution in thylakoids and Photosystem II particles from Synechococcus PC 7942. The significance of the reactivation kinetics is discussed. Reactivation by Ca2+ was inhibited by antibodies to mammalian calmodulin, indicating that the binding site in Photosystem II may be analogous to that of this protein.

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Abbreviations

HEPES:

n-2-Hydroxyethylpiperazine-ń-2-ethane sulphonic acid

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Tramontini, L.S., McColl, S. & Hilary Evans, E. Ca2+ and Mg2+-binding and a putative calmodulin type Ca2+-binding site in Synechococcus Photosystem II. Photosynth Res 50, 233–241 (1996). https://doi.org/10.1007/BF00033122

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