Comparative stability studies on the iron and manganese forms of the cambialistic superoxide dismutase from Propionibacterium shermanii

B Meier; F Parak; A Desideri; G Rotilio

doi:10.1016/s0014-5793(97)00960-5

Comparative stability studies on the iron and manganese forms of the cambialistic superoxide dismutase from Propionibacterium shermanii

FEBS Lett. 1997 Sep 1;414(1):122-4. doi: 10.1016/s0014-5793(97)00960-5.

Authors

B Meier¹, F Parak, A Desideri, G Rotilio

Affiliation

¹ Fakultät für Physik E17, Technische Universität München, Garching, Germany.

PMID: 9305744
DOI: 10.1016/s0014-5793(97)00960-5

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.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Ammonium Sulfate / pharmacology
Binding Sites
Circular Dichroism
Electron Spin Resonance Spectroscopy
Enzyme Stability
Hot Temperature
Hydrogen-Ion Concentration
Iron / metabolism*
Manganese / metabolism*
Propionibacterium / enzymology*
Protein Denaturation
Spectrophotometry
Superoxide Dismutase / chemistry
Superoxide Dismutase / metabolism*

Substances

Manganese
Iron
Superoxide Dismutase
Ammonium Sulfate