Please use this identifier to cite or link to this item: https://www.um.edu.mt/library/oar/handle/123456789/117863
Title: A single mutation is sufficient to modify the metal selectivity and specificity of a eukaryotic manganese superoxide dismutase to encompass iron
Authors: Hunter, Thérèse
Bonetta, Rosalin
Sacco, Anthony
Vella, Marita
Sultana, Paul-Michael
Trinh, Chi H.
Fadia, Hava B. R.
Borowski, Tomasz
Garcia-FandiÇo, Rebeca
Stockner, Thomas
Hunter, Gary J.
Keywords: Eukaryotic cells
Manganese
Superoxides
Enzymes
Metalloproteins
Issue Date: 2018
Publisher: Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
Citation: Hunter, T., Bonetta, R., Sacco, A., Vella, M., Sultana, P. M., Trinh, C. H.,...Hunter, G. J. (2018). A single mutation is sufficient to modify the metal selectivity and specificity of a eukaryotic manganese superoxide dismutase to encompass iron. Chemistry–A European Journal, 24(20), 5303-5308.
Abstract: 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 Umg-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.
URI: https://www.um.edu.mt/library/oar/handle/123456789/117863
Appears in Collections:Scholarly Works - InsESRSF



Items in OAR@UM are protected by copyright, with all rights reserved, unless otherwise indicated.