Complete amino acid sequence of 33 kDa protein isolated from spinach photosystem II particles

Abstract
The amino acid sequence of the 33 kDa protein isolated as an extrinsic protein from spinach photosystem II particles was determined by using solid‐phase sequencing and conventional procedures. The 33 kDa protein was found to be composed of 248 amino acid residues, to lack histidine and to have a molecular mass of 26 663 Da, which was considerably smaller than the value deduced from SDS‐polycrylamide gel electrophoresis. The sequence of the 33 kDa protein was compared with those of the bacterial Superoxide dismutases (SOD) with Mn atoms at an active site. A part of the sequence of the 33 kDa protein was similar to a region in Mn‐SODs from Bacillus stearothermophilus and Escherichia coli, which was expected to be the Mn‐binding site.

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