Dioxygen activation by copper, heme and non-heme iron enzymes: comparison of electronic structures and reactivities.
Enzymes containing heme, non-heme iron and copper active sites play important roles in the activation of dioxygen for substrate oxidation. One key reaction step is CH bond cleavage through H-atom abstraction. On the basis of the ligand environment and the redox properties of the metal, these enzymes employ different methods of dioxygen activation. Heme enzymes are able to stabilize the very reactive iron(IV)-oxo porphyrin-radical intermediate. This is generally not accessible for non-heme iron systems, which can instead use low-spin ferric-hydroperoxo and iron(IV)-oxo species as reactive oxidants. Copper enzymes employ still a different strategy and achieve H-atom abstraction potentially through a superoxo intermediate. This review compares and contrasts the electronic structures and reactivities of these various oxygen intermediates.
Decker
Andrea
A
Department of Chemistry, Stanford University, Stanford, California 94305, USA.
Solomon
Edward I
EI
D001665:Binding Sites; D002384:Catalysis; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D004798:Enzymes / Q000737:chemistry*; D006418:Heme / Q000737:chemistry*; D006860:Hydrogen Bonding; D019159:Nonheme Iron Proteins / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D011487:Protein Conformation
D004798:Enzymes; D019159:Nonheme Iron Proteins; D006418:Heme; D003300:Copper; D010100:Oxygen