A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron

We have generated a site‐directed mutant of the manganese superoxide dismutase SOD‐3 of C.elegans (MnSOD‐3) which modifies the metal specificity of the enzyme. While wild‐type MnSOD‐3 functions with manganese in the active site (3600 U mg(−1) of protein) it has little or no activity when iron is inc...

Descripción completa

Detalles Bibliográficos
Autores principales: Hunter, Thérèse, Bonetta, Rosalin, Sacco, Anthony, Vella, Marita, Sultana, Paul‐Michael, Trinh, Chi H., Fadia, Hava B. R., Borowski, Tomasz, Garcia‐Fandiño, Rebeca, Stockner, Thomas, Hunter, Gary J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Full Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5969255/
https://www.ncbi.nlm.nih.gov/pubmed/29178484
http://dx.doi.org/10.1002/chem.201704655
Descripción
Sumario:We have generated a site‐directed mutant of the manganese superoxide dismutase SOD‐3 of C.elegans (MnSOD‐3) which modifies the metal specificity of the enzyme. While wild‐type MnSOD‐3 functions with manganese in the active site (3600 U mg(−1) of protein) it has little or no activity when iron is incorporated. However, when histidine replaces glutamine 142 in the active site, the enzyme retains 50 % of its activity and becomes cambialistic for its metal cofactor exhibiting very similar specific activity with either manganese or iron.

Ejemplares similares