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

FEBS Letters

Meier, Beate¹  Rotilio, Giuseppe²  Desideri, Alessandro²  Parak, Fritz¹ 

[1] Fakultät für Physik E17, Technische Universität München, James-Franck-Straße, D-85747 Garching, Germany;Dipartimento di Biologia, Università di Roma, Tor Vergata, Viale della Ricerca Scientifica, I-00133 Rome, Italy

关键词: Superoxide dismutase;    pH stability;    Thermal stability;    (Propionibacterium shermanii);    SOD;    superoxide dismutase;    Fe-SOD;    iron-containing SOD;    Mn-SOD;    manganese-containing SOD;    Cu;    Zn-SOD;    copper- and zinc-containing SOD;    Ni-SOD;    nickel-containing SOD;    P. shermanii;    Propionibacterium freudenreichii sp. shermanii;   

DOI  :  10.1016/S0014-5793(97)00960-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown