Dioxygen activation at non-heme iron: insights from rapid kinetic studies.
One of the common biochemical pathways of binding and activation of dioxygen involves non-heme iron centers. The enzyme cycles usually start with an iron(II) or diiron(II) state and traverse via several intermediates (detected or postulated) such as (di)iron(III)-superoxo, (di)iron(III)-(hydro)peroxo, iron(III)iron(IV)-oxo, and (di)iron(IV)-oxo species, some of which are responsible for substrate oxidation. In this Account, we present results of kinetic and mechanistic studies of dioxygen binding and activation reactions of model inorganic iron compounds. The number of iron centers, their coordination number, and the steric and electronic properties of the ligands were varied in several series of well-characterized complexes that provided reactive manifolds modeling the function of native non-heme iron enzymes. Time-resolved cryogenic stopped-flow spectrophotometry permitted the identification of kinetically competent intermediates in these systems. Inner-sphere mechanisms dominated the chemistry of dioxygen binding, intermediate transformations, and substrate oxidation as most of these processes were controlled by the rates of ligand substitution at the iron centers.
Korendovych
Ivan V
IV
Department of Chemistry, Tufts University, Medford, Massachusetts 02155, USA.
Kryatov
Sergey V
SV
Rybak-Akimova
Elena V
EV
D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000378:metabolism; D007501:Iron / Q000737:chemistry*; D058085:Iron Compounds / Q000737:chemistry*; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D019159:Nonheme Iron Proteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
D058085:Iron Compounds; D008024:Ligands; D019159:Nonheme Iron Proteins; C066317:ferryl iron; D006861:Hydrogen Peroxide; D007501:Iron; D010100:Oxygen