Comparative stability studies on the iron and manganese forms of the cambialistic superoxide dismutase from Propionibacterium shermanii
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Published on: March 24, 2012
1Fakultät für Physik E17, Technische Universität München, Garching, Germany.
FEBS Letters
|September 26, 1997
Abstract:
The superoxide dismutase of Propionibacterium shermanii shows similar activity with iron and manganese bound at the active site of the protein. On the other hand, the iron form, in comparison to the manganese form, exhibits higher stability towards thermal- and pH-dependent inactivation. Upon inactivation the metal ions are released from the active site. Thus, in comparison to the manganese form, a higher stability of the iron-protein complex might be the triggering reason for this behavior.

