Regeneration of the high-affinity manganese-binding site in the reaction center of an oxygen-evolution deficient mutant of Scenedesmus by protease action

1989 ◽  
Vol 22 (1) ◽  
pp. 101-113 ◽  
Author(s):  
Christopher Preston ◽  
Michael Seibert
2002 ◽  
Vol 57 (9-10) ◽  
pp. 853-857 ◽  
Author(s):  
Kvetoslava Burda ◽  
Jerzy Kruk ◽  
Kazimierz Strzalka ◽  
Georg H. Schmid

We have found that Copper(II) ions at about equimolar Cu2+/photosystem II (PS II) reaction center proportions stimulate oxygen evolution nearly twofold. This high affinity Cubinding site is different from the binding sites of Mn and Ca ions. The analysis of the Cu2+ content in PS II preparations isolated from wild-type tobacco and a tobacco mutant deficient in light-harvesting complex suggests that Cu2+ may be a native component of PS II and may take part in the oxygen evolution process. At higher concentrations, Cu2+ ions inhibit oxygen evolution and quench fluorescence.


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