Abstract
This chapter describes the involvement of polypeptides in photosynthetic oxygen evolution. The involvement of protein components in the oxygen evolving reactions have often been suggested from correlations between inhibition and alteration or removal of certain proteins. In an experimented discussed in the chapter, the inhibition of oxygen evolution in inside-out thylakoids obtained by salt washing was accompanied by a release of mainly two polypeptides, the 17 kDa and 23 kDa polypeptides, as revealed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Contrary to Tris-treatments neither Mn nor the 34 kDa polypeptide were released. When washed inside-out thylakoids were incubated under low ionic strength with the crude chloroplast extract, only the 17 kDa and 23 kDa polypeptides were bound to the inner thylakoid surface concomitant with a reconstitution of oxygen evolution. There are similarities in the protein release pattern from inside-out thylakoids and from PS II particles obtained by detergent treatment of thylakoids, suggesting that the PS II detergent particles expose the original inner side of the membrane.
Published Version
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