[go: up one dir, main page]

Mansuy, 2007 - Google Patents

A brief history of the contribution of metalloporphyrin models to cytochrome P450 chemistry and oxidation catalysis

Mansuy, 2007

View HTML
Document ID
2921717126115406245
Author
Mansuy D
Publication year
Publication venue
Comptes Rendus Chimie

External Links

Snippet

Since their discovery in the 1960s, cytochrome P450-dependent monooxygenases have very much attracted the interest of chemists because of their ability to catalyze the selective transfer of an oxygen atom from O2 to very diverse substrates including alkanes. The huge …
Continue reading at www.sciencedirect.com (HTML) (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07DHETEROCYCLIC COMPOUNDS
    • C07D487/00Heterocyclic compounds containing nitrogen atoms as the only ring hetero atoms in the condensed system, not provided for by C07D451/00 - C07D477/00
    • C07D487/22Heterocyclic compounds containing nitrogen atoms as the only ring hetero atoms in the condensed system, not provided for by C07D451/00 - C07D477/00 in which the condensed system contains four or more hetero rings
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07DHETEROCYCLIC COMPOUNDS
    • C07D487/00Heterocyclic compounds containing nitrogen atoms as the only ring hetero atoms in the condensed system, not provided for by C07D451/00 - C07D477/00
    • C07D487/02Heterocyclic compounds containing nitrogen atoms as the only ring hetero atoms in the condensed system, not provided for by C07D451/00 - C07D477/00 in which the condensed system contains two hetero rings
    • C07D487/08Bridged systems
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07DHETEROCYCLIC COMPOUNDS
    • C07D487/00Heterocyclic compounds containing nitrogen atoms as the only ring hetero atoms in the condensed system, not provided for by C07D451/00 - C07D477/00
    • C07D487/02Heterocyclic compounds containing nitrogen atoms as the only ring hetero atoms in the condensed system, not provided for by C07D451/00 - C07D477/00 in which the condensed system contains two hetero rings
    • C07D487/04Ortho-condensed systems
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07DHETEROCYCLIC COMPOUNDS
    • C07D487/00Heterocyclic compounds containing nitrogen atoms as the only ring hetero atoms in the condensed system, not provided for by C07D451/00 - C07D477/00
    • C07D487/12Heterocyclic compounds containing nitrogen atoms as the only ring hetero atoms in the condensed system, not provided for by C07D451/00 - C07D477/00 in which the condensed system contains three hetero rings
    • C07D487/14Ortho-condensed systems

Similar Documents

Publication Publication Date Title
Mansuy A brief history of the contribution of metalloporphyrin models to cytochrome P450 chemistry and oxidation catalysis
Van Stappen et al. Designing artificial metalloenzymes by tuning of the environment beyond the primary coordination sphere
Louka et al. Catalytic mechanism of aromatic nitration by cytochrome P450 TxtE: involvement of a ferric-peroxynitrite intermediate
Kal et al. Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants
Hrycay et al. Monooxygenase, peroxidase and peroxygenase properties and reaction mechanisms of cytochrome P450 enzymes
Oohora et al. Myoglobins engineered with artificial cofactors serve as artificial metalloenzymes and models of natural enzymes
Mukherjee et al. Inspiration from nature: influence of engineered ligand scaffolds and auxiliary factors on the reactivity of biomimetic oxidants
Huang et al. Beyond ferryl-mediated hydroxylation: 40 years of the rebound mechanism and C–H activation
Costas et al. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates
Meunier et al. Active iron-oxo and iron-peroxo species in cytochromes P450 and peroxidases; oxo-hydroxo tautomerism with water-soluble metalloporphyrins
Huang et al. Oxygen activation and radical transformations in heme proteins and metalloporphyrins
Mukherjee et al. Electron transfer control of reductase versus monooxygenase: Catalytic C–H bond hydroxylation and alkene epoxidation by molecular oxygen
Mansuy et al. Chemical model systems for drug-metabolizing cytochrome-P-450-dependent monooxygenases
Cooper et al. Molecular probes of the mechanism of cytochrome P450. Oxygen traps a substrate radical intermediate
Modi et al. Oxidizing intermediates in P450 catalysis: a case for multiple oxidants
Ghosh et al. Selective C–H bond oxidation catalyzed by the Fe-bTAML complex: Mechanistic implications
Makris et al. Activation of molecular oxygen by cytochrome P450
Denisov et al. Activation of molecular oxygen in cytochromes P450
Bassan et al. Theoretical studies of enzyme mechanisms involving high-valent iron intermediates
Reiter et al. Accordion porphyrins: Hybrid models for heme and binuclear monooxygenases
Nayek et al. Bioinorganic chemistry on electrodes: methods to functional modeling
Samokyszyn et al. Topology of the chloroperoxidase active site: regiospecificity of heme modification by phenylhydrazine and sodium azide
Alexander et al. Chemicals, cancer, and cytochrome P-450
Othman et al. Hydroxylation of diclofenac: an illustration of the complementary roles of biomimetic metalloporphyrin catalysts and yeasts expressing human cytochromes P450 in drug metabolism studies
Mansuy Biocatalysis and substrate chemodiversity: Adaptation of aerobic living organisms to their chemical environment