The carboxyl-terminal tripeptide of the manganese-stabilizing protein is required for quantitative assembly into photosystem II and for high rates of oxygen evolution activity

A study was conducted to examine the in vitro reconstitution of spinach photosystem II with recombinant manganese stabilizing protein supporting C-terminal deletions of amino acids. Oxygen evolution activity was determined polarographically at 25 degrees C while size-exclusion chromatography was carried out to determine the molecular masses of wild-type and mutant proteins. Results suggested that mutational effects on the binding and role of the protein may be correlated with tertiary structural changes.