The chloroplast reductase-binding protein is identical to the 16.5-kDa polypeptide described as a component of the oxygen-evolving complex.

The N-terminal sequence of the spinach chloroplast reductase-binding protein was determined. The sequence is the same one of a 16.5-kDa polypeptide described as a component of the oxygen-evolving system. Antibodies against both proteins are equivalent as shown by immunoblots, Ouchterlony assays, precipitation of reductase-binding protein complex, and agglutination of thylakoids partially depleted of reductase. These results suggest both proteins are identical. Exposure of the binding protein on the stromal side of thylakoids is supported by agglutination of thylakoids partially depleted of reductase, proteolysis by trypsin, and by accessibility to Fab of anti-binding protein. The latter prevents rebinding of reductase supporting the functional role of the binding protein (16.5 kDa).