Abstract
Chloroplast membranes have been shown previously to undergo a change in radioactive labeling by chemical modification reagents that is dependent on electron transport and protolytic events in Photosystem II. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis has been used to show that a low molecular weight chloroplast polypeptide (7.2 Kilodaltons) undergoes the most change in acetic anhydride labeling upon Photosystem II electron transport. A similar polypeptide has been identified by other workers as a component of the hydrophobic trans-membrane proton channel in chloroplasts. Photosystem I electron transport does not give the change in level of incorporation of acetic anhydride into this membrane protein. These results suggest that protons liberated from Photosystem II interact with a hydrophobic portion of the chloroplast membrane, perhaps with the trans-membrane proton channel.
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