ABSTRACT
An Fe(III)-superoxide-Cu(I) cytochrome c oxidase model reacts intermolecularly with hindered phenols leading to phenoxyl radicals, as was observed in the enzyme and evidence for the formation of an Fe(IV)-oxo is presented.
Subject(s)
Copper/chemistry , Electron Transport Complex IV/chemistry , Ferric Compounds/chemistry , Superoxides/chemistry , Tyrosine/chemistry , Binding Sites , Cations , Copper/metabolism , Electron Transport Complex IV/metabolism , Enzyme Activation , Ferric Compounds/metabolism , Free Radicals , Models, Molecular , Molecular Mimicry , Organometallic Compounds/chemical synthesis , Phenols/chemistry , Spectrum Analysis , Superoxides/metabolismABSTRACT
A new approach to the synthesis of Rh(III) corrole complexes is developed and an unusual activation of C-C and C-N bonds is disclosed.
ABSTRACT
Electrocatalytic reduction of a series of chemical oxidants of different power (tert-butyl hydroperoxide, potassium peroxomonosulfate, peracetic acid, and m-chloroperbenzoic acid) at iron-porphyrin-modified graphite electrodes is studied in buffered aqueous solutions by rotating disk and ring-disk voltammetry. Both ferric and ferrous porphyrins are catalytically active. Turnover of ferric catalysts is slower than that of the ferrous analogues and involves competing catalytic reduction and disproportionation. The kinetic data are consistent with reactant binding being the rate-determining step in catalysis by Fe(III). In catalysis by Fe(II), the turnover is controlled by the first electron transfer. The covalently linked proximal imidazole ligand is found to be crucial for achieving the Fe(III) catalysis.
Subject(s)
Carboxylic Acids/chemistry , Ferric Compounds/chemistry , Ferrous Compounds/chemistry , Metalloporphyrins/chemistry , Catalysis , Electrochemistry , Kinetics , Oxidation-Reduction , Peroxides/chemistrySubject(s)
Electron Transport Complex IV/chemistry , Hemoglobins/metabolism , Myoglobin/analogs & derivatives , Myoglobin/metabolism , Copper/metabolism , Heme/chemistry , Heme/metabolism , Humans , Hydrogen-Ion Concentration , Iron/metabolism , Models, Molecular , Molecular Structure , Myoglobin/chemical synthesis , Oxygen/metabolismABSTRACT
A superstructured tetraphenylporphyrin with a covalently attached proximal imidazole axial base and three distal imidazole pickets has been developed as a model for the active site of terminal oxidases such as cytochrome c oxidase. The oxygen adduct of the Fe-only heme (at low temperature) has a diamagnetic NMR and is EPR silent, which taken together with a resonance Raman oxygen isotope sensitive band (nuFe-O) at 575/554 cm-1 (16O2/18O2) indicates formation of a six-coordinate heme-superoxide complex. Unexpectedly, the Fe/Cu complex, where the copper is in a trisimidazole environment approximately 5 A above the heme plane, displays similar characteristics: a diamagnetic NMR, EPR silence, and nuFe-O at 570/544 cm-1. This indicates the dioxygen adduct of this Fe/Cu system is also a superoxide. This contrasts with previously characterized partially reduced dioxygen intermediates of binuclear heme/copper complexes that form Fe/Cu mu-peroxo complexes.
Subject(s)
Copper/chemistry , Electron Transport Complex IV/chemistry , Heme/chemistry , Superoxides/chemistry , Biomimetic Materials/chemistry , Copper/metabolism , Electron Transport Complex IV/metabolism , Ferric Compounds/chemistry , Heme/metabolism , Models, Chemical , Nuclear Magnetic Resonance, Biomolecular , Oxidation-Reduction , Oxygen/chemistry , Oxygen/metabolism , Spectrum Analysis, Raman , Superoxides/metabolismABSTRACT
The electrochemical behavior of multilayer films formed by iron porphyrins deposited on an edge plane graphite electrode has been examined under anaerobic conditions. In the scan rate interval (1-250 mV/s) where the electrode reaction is reversible, CV diagrams of these films demonstrate substantial deviations from ideality in broadening and separation of the peaks. A model that describes the observed behavior is proposed by taking into account the potential distribution at the electrode/film interface and the concentration dependence of surface activity coefficients. The peak separation is described in terms of the electric double layer that affects the potential difference driving the electrode reaction. The effective potential difference deviates from the applied value due to the potential distribution across the film. The interfacial potential distribution depends on the ionic concentration inside the film. When different ionic concentrations are assumed for oxidation and reduction, different shifts from the applied potential lead to a hysteresis of the peaks. The peak broadening is modeled by using the lattice theory expression for the surface activity coefficients. The model shows that the midpoint potentials of the redox centers depend on the ionic concentration inside the film. At low ionic concentrations, they are remarkably close to the midpoints of the cytochrome c oxidase heme a3/CuB site.
Subject(s)
Electrochemistry , Heme/chemistry , Electrodes , Electron Transport Complex IV/chemistry , Molecular Mimicry , Oxidation-ReductionABSTRACT
Cobalt(II) porphyrins were studied to determine the influence of distal site metalation and superstructure upon dioxygen reactivity in active site models of cytochrome c oxidase (CcO). Monometallic, Co(II)(P) complexes when ligated by an axial imidazole react with dioxygen to form reversible Co-superoxide adducts, which were characterized by EPR and resonance Raman (RR). Unexpectedly, certain Co porphyrins with Cu(I) metalated imidazole pickets do not form mu-peroxo Co(III)/Cu(II) products even though the calculated intermetallic distance suggests this is possible. Instead, cobalt-porphyrin-superoxide complexes are obtained with the distal copper remaining as Cu(I). Moreover, distal metals (Cu(I) or Zn(II)) greatly enhance the stability of the dioxygen adduct, such that Co superoxides of bimetallic complexes demonstrate minimal reversibility. The "trapping" of dioxygen by a second metal is attributed to structural and electrostatic changes within the distal pocket upon metalation. EPR evidence suggests that the terminal oxygen in these bimetallic Co-superoxide systems is H-bonded to the NH of an imidazole picket amide linker, which may contribute to enthalpic stabilization of the dioxygen adduct. Stabilization of the dioxygen adduct in these bimetallic systems suggests one possible role for the distal copper in the Fe/Cu bimetallic active site of terminal oxidases, which form a heme-superoxide/copper(I) adduct upon oxygenation.
Subject(s)
Cobalt/chemistry , Electron Transport Complex IV/chemistry , Metalloporphyrins/chemical synthesis , Binding Sites , Catalysis , Copper/chemistry , Electron Spin Resonance Spectroscopy , Kinetics , Models, Molecular , Molecular Conformation , Molecular Structure , Oxidation-Reduction , Oxygen/chemistry , Spectrum Analysis, RamanSubject(s)
Carbon Monoxide/pharmacology , Copper/chemistry , Cyanides/pharmacology , Electron Transport Complex IV/antagonists & inhibitors , Electron Transport Complex IV/chemistry , Heme/chemistry , Animals , Binding Sites , Carbon Monoxide/metabolism , Catalysis , Cattle , Copper/metabolism , Cyanides/metabolism , Electron Transport Complex IV/metabolism , Heme/metabolism , Ions/chemistry , Ions/metabolism , Iron/metabolism , Molecular Structure , Oxidation-Reduction , Oxygen/metabolismABSTRACT
Catalytic reduction of O(2) and H(2)O(2) by new synthetic analogues of the heme/Cu site in cytochrome c and ubiquinol oxidases has been studied in aqueous buffers. Among the synthetic porphyrins yet reported, those employed in this study most faithfully mimic the immediate coordination environment of the Fe/Cu core. Under physiologically relevant conditions, these biomimetic catalysts reproduce key aspects of the O(2) and H(2)O(2) chemistry of the enzyme. When deposited on an electrode surface, they catalyze the selective reduction of O(2) to H(2)O at potentials comparable to the midpoint potential of cytochrome c. The pH dependence of the half-wave potentials and other data are consistent with O-O bond activation at these centers proceeding via a slow generation of a formally ferric-hydroperoxo intermediate, followed by its rapid reduction to the level of water. This kinetics is analogous to that proposed for the O-O reduction step at the heme/Cu site. It minimizes the steady-state concentration of the catalytic intermediate whose decomposition would release free H(2)O(2). The maximum catalytic rate constants of O(2) reduction by the ferrous catalyst and of H(2)O(2) reduction by both ferric and ferrous catalysts are comparable to those reported for cytochrome oxidase. The oxidized catalyst also displays catalase activity. Comparison of the catalytic properties of the biomimetic complexes in the FeCu and Cu-free forms indicates that, in the regime of rapid electron flux, Cu does not significantly affect the turnover frequency or the stability of the catalysts, but it suppresses superoxide-releasing autoxidation of an O(2)-catalyst adduct. The distal Cu also accelerates O(2) binding and minimizes O-O bond homolysis in the reduction of H(2)O(2).
Subject(s)
Copper/chemistry , Electron Transport Complex IV/chemistry , Heme/analogs & derivatives , Oxygen/chemistry , Binding Sites , Catalysis , Electrochemistry , Electron Transport Complex IV/metabolism , Hydrogen Peroxide/chemistry , Hydrogen Peroxide/metabolism , Hydrogen-Ion Concentration , Kinetics , Molecular Mimicry , Organometallic Compounds/chemistry , Oxidation-Reduction , Oxygen/metabolismABSTRACT
We measured the redox stoichiometry and rate constants for the electrochemical reduction of ClO(2)(-) at pH 7, catalyzed by a series of metalloporphyrins of Mn, Fe, and Co with different proximal and distal environments. A clean four-electron reduction was observed. The catalytic activity correlates well with that observed in reduction of H(2)O(2). The axial imidazole and/or a redox-active distal metal (Cu or Co) increases the turnover frequency in several compounds. The metalloporphyrins were inert to ClO(x)(-) (x = 3,4) and IO(3)(-) but catalyzed facile two-electron reduction of IO(4)(-); six-electron reduction of BrO(3)(-) was also observed.
Subject(s)
Chlorides/chemistry , Metalloporphyrins/chemistry , Catalysis , Electrochemistry , Kinetics , Oxidation-ReductionABSTRACT
Three biomimetic models for the binuclear Fe/Cu (heme/trisimidazole) active site of terminal oxidases, such as cytochrome c oxidase and related enzymes, have been prepared. Based upon a tetrakis(aminophenyl)porphyrin core, these models possess a single covalently linked imidazole-bearing tail on one side of the porphyrin and three imidazole "pickets" on the opposite side of the porphyrin ring. Three different imidazole picket motifs are characterized in free base, Fe, Zn, Fe/Cu, and Zn/Cu forms. A combination of NMR, EPR, and IR demonstrates that, for the N-methylimidazole systems studied, the distal Cu is bound within the trisimidazole environment in the reduced (Cu(I)) and oxidized (Cu(II)) forms. The imidazole picket substitution pattern and state of metalation have significant influence on the interaction of these compounds with CO. For imidazole picket systems containing NH groups, intramolecular H bonds compete with Cu(I) coordination of the N donors.