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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 |
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A_single_mutation_is_sufficient_to_modify_the_metal_selectivity_and_specificity_of_a_eukaryotic_manganese_superoxide_dismutase_to_encompass_iron_2018.pdf | 836.11 kB | Adobe PDF | View/Open |
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