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An L-amino acid oxidase with high specifity for basic L-amino acids was isolated from the cyanobacterium Synechococcus PCC 7942, and the enzyme was partially characterized. This enzyme was compared to the previously described L-amino acid oxidase from Synechococcus PCC6301 (G. Wälzlein, A. E. Gau, and E. K. Pistorius, Z. Naturforsch. 43c, 5 4 5-553, 1988). In addition, photosystem II complexes were isolated from Synechococcus PCC 7942, and it could be shown that a 36 kDa polypeptide which crossreacts with the antiserum raised against the L-amino acid oxidase (50 kD a) is present in isolated PS II complexes from Synechococcus PCC 7942 as already shown to be the case for Synechococcus PC C 6301 (A. E. Gau, G. W älzlein, S. Gärtner, M. Kuhlmann, S. Specht, and E. K. Pistorius, Z. Naturforsch. 44c, 9 7 1 -9 7 5 , 1989). These results clearly show that in isolated photosystem II complexes from Synechococcus PCC 6301 as well as PCC 7942 a fourth polypeptide (besides D 1, D 2 and the manganese stabilizing protein) is present in the 30 kDa region and support our hypothesis suggesting that the water oxidizing enzyme is a separate protein (distinct from D 1 and D 2)

Isolation And Partial Characterization Of An L -Amino Acid Oxidase And Of Photosystem Ii Complexes From The Cyanobacterium Synechococcus PCC7942