biostudies-literatureHunter TUniversity of MaltaBiotechnology and Biological Sciences Research Council5303-5308https://www.ebi.ac.uk/biostudies/studies/S-EPMC5969255biostudies-literatureUnknown24(20)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.Chemistry (Weinheim an der Bergstrasse, Germany)A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron.PMC5969255PHBIN02-1PHBRP03-17PHBRP03-05BB/L015056/1Hunter TTrinh CHFadia HBRBorowski TStockner THunter GJBonetta RVella MSultana PMGarcia-Fandino RSacco AfalseA 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 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.2018-01-01T00:00:00Z2018 Apr2026-05-03T02:14:30.405Z2026-04-07T18:44:06.018ZS-EPMC59692552917848410.1002/chem.201704655