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Comparative stability studies on the iron and manganese forms of the cambialistic superoxide dismutase from Propionibacterium shermanii
Author(s) -
Meier Beate,
Parak Fritz,
Desideri Alessandro,
Rotilio Giuseppe
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00960-5
Subject(s) - propionibacterium , manganese , superoxide dismutase , chemistry , biology , biochemistry , microbiology and biotechnology , bacteria , enzyme , genetics , organic chemistry
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.