1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	A metalloprotein. Enzymes from most eukaryotes contain both copper and zinc, those from mitochondria and most prokaryotes contain manganese or iron. ligand binding site and structure	-, 438186, 438189, 438190	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	active site is not conserved, differing from others of Mn-SOD and Fe-SOD	438096	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	active site, manganese-binding site and contact site between monomers	-, 438096	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	amino acid composition, comparison	-, 438113, 438116, 438128, 438129, 438134, 438142, 438145, 438147, 438153, 438157, 438162, 438166, 438167, 438177, 438182, 438184	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	amino acid sequence alignment and comparison	-, 438096, 438141, 438171, 438173, 438179, 438187, 438188, 438189, 438190	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	Cu2+-binding	438123	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	electrostatic guidance of anionic substrate to the active site, detailed overview. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis	745653	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	mechanism	-, 438096, 438097, 438122, 438125, 438126	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	presence of a general acid and a general base in catalysis. Catalytic model requires histidine residues, metal-bound water molecules and two hydrated metal ions to operate in concert	675243	
1.15.1.1	2 superoxide + 2 H+ = O2 + H2O2	the amino acid residues His46, His48, His63, His71, His80, and His120, and Asp83 in the active site are conserved as in other Cu/ZnSODs	-, 690078