title: Comparative studies on a superoxide dismutase exhibiting enzymatic activity with iron and manganese as active cofactor.
abstract: The SOD of Propionibacterium freudenreichii, ssp. shermanii belongs to a new group of SOD's capable of retaining activity with either Fe or Mn as active metal cofactor. Both enzymes exhibit identical secondary structure and immunological determinants. Hydrogen peroxide irreversibly inhibits both enzymes. The protein moiety of the Fe- and Mn-SOD could be digested with trypsin to a single active fragment.
authors.affiliation: Chemisches Institut, Tieräztliche Hochschule, Hannover, FRG.
authors.forename: B
authors.initials: B
authors.lastname: Meier
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002942:Circular Dichroism; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007501:Iron / Q000378:metabolism*; D008345:Manganese / Q000378:metabolism*; D011424:Propionibacterium / Q000201:enzymology; D011489:Protein Denaturation; D013482:Superoxide Dismutase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D013481:Superoxides / Q000378:metabolism; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D013481:Superoxides; D008345:Manganese; D006861:Hydrogen Peroxide; D007501:Iron; D013482:Superoxide Dismutase