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• W2068296286 abstract "Inside-out spinach thylakoid vesicles have been used for inhibition and reconstitution of photosynthetic water splitting. Washing inside-out vesicles with a buffer containing 250 mM NaCl inhibited 75% of the Photosystem II reduction of phenyl-p-benzoquinone. In contrast, the same treatment of right-side-out vesicles gave quite a small inhibition. The site of inhibition was shown by fluorescence induction to be located at the water-splitting side of P-680. The salt-induced inhibition was accompanied by the release of two polypeptides (23 and 16 kDa) from the inner thylakoid surface. Readdition of the salt-washed supernatant or a crude chloroplast extract to the washed inside-out vesicles at low ionic strength gave a 2.7-fold stimulation of the water-splitting activity, thereby restoring about 60% of the activity lost by salt washing. This stimulation was abolished by proteolysis of the reconstituting fractions. Restoration of the water-splitting reaction was accompanied by rebinding of the 23 and 16 kDa polypeptides to the inside-out vesicles. After polypeptide purification by ion-exchange chromatography it was shown that the 23kDa polypeptide was responsible for the restorative effect. These observations provide strong evidence that the 23 kDa polypeptide, electrostatically bound to the inner thylakoid surface, is involved in the photosynthetic water-splitting reaction." @default.
• W2068296286 created "2016-06-24" @default.
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• W2068296286 date "1982-07-01" @default.
• W2068296286 modified "2023-09-26" @default.
• W2068296286 title "Reconstitution of photosynthetic water splitting in inside-out thylakoid vesicles and identification of a participating polypeptide" @default.
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• W2068296286 doi "https://doi.org/10.1016/0005-2728(82)90271-7" @default.
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