Molecular Properties of the Manganese Enzymes

Much less information is available on the manganese superoxide dismutases. No crystal structure has been reported for such an enzyme, but similarities in the three-dimensional structures can be deduced from the Cd-spectra and comparisons 

Due to the relatively low metal-binding constants compared to the Cu Znj-SOD s, the metal contents of isolated manganese superoxide dismutases are varying between 1.0 and 2.0 g atoms per dimer Remarkable differences are also found in the 

The amino acid sequences of mangano SOD s have been extensively studied The N-terminal residues indicate a high degree of sequence homology between iron and manganese enzymes. Prediction of the secondary structure of the manganese enzymes from the amino acid sequences and comparison with the secondary structure obtained for the iron enzyme reveals that the oc-heUces and -strands align quite well. 

Most of the current work on manganese superoxide dismutases is limited on purification studies of these unique class of enzymes Recently the joint puri- 

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