Comparative stability studies on the iron and manganese forms of the cambialistic superoxide dismutase from Propionibacterium shermanii.
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.
Meier
B
B
Fakultät für Physik E17, Technische Universität München, Garching, Germany.
Parak
F
F
Desideri
A
A
Rotilio
G
G
D000645:Ammonium Sulfate / Q000494:pharmacology; D001665:Binding Sites; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000378:metabolism*; D008345:Manganese / Q000378:metabolism*; D011424:Propionibacterium / Q000201:enzymology*; D011489:Protein Denaturation; D013053:Spectrophotometry; D013482:Superoxide Dismutase / Q000737:chemistry / Q000378:metabolism*
D008345:Manganese; D007501:Iron; D013482:Superoxide Dismutase; D000645:Ammonium Sulfate