Self-assembly of the oxy-tyrosinase core and the fundamental components of phenolic hydroxylation.
about
Nitric oxide activation by distal redox modulation in tetranuclear iron nitrosyl complexesStructure/function correlations among coupled binuclear copper proteins through spectroscopic and reactivity studies of NspF.Copper-Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity.HHM motif at the CuH-site of peptidylglycine monooxygenase is a pH-dependent conformational switch.Catalytic phenol hydroxylation with dioxygen: extension of the tyrosinase mechanism beyond the protein matrix.Mechanism of copper(I)/TEMPO-catalyzed aerobic alcohol oxidationHigh-valent copper in biomimetic and biological oxidations.A "naked" Fe(III)-(O₂²⁻)-Cu(II) species allows for structural and spectroscopic tuning of low-spin heme-peroxo-Cu complexes.Formation of hybrid guanidine-stabilized bis(μ-oxo)dicopper cores in solution: Electronic and steric perturbations.Simplest Monodentate Imidazole Stabilization of the oxy-Tyrosinase Cu2 O2 Core: Phenolate Hydroxylation through a Cu(III) Intermediate.Theoretical study of the oxidation of phenolates by the [Cu2O2(N,N'-di-tert-butylethylenediamine)2]2+ complex.Record Broken: A Copper Peroxide Complex with Enhanced Stability and Faster Hydroxylation Catalysis.The Cu2O2 torture track for a real-life system: [Cu2(btmgp)2O2](2+) oxo and peroxo species in density functional calculations.Catalytic aerobic oxidation of phenols to ortho-quinones with air-stable copper precatalysts.Bioinspired copper(I) complexes that exhibit monooxygenase and catechol dioxygenase activity.De Novo Design of Tetranuclear Transition Metal Clusters Stabilized by Hydrogen-Bonded Networks in Helical Bundles.Metal carbonate complexes formed through the capture of ambient O2 and CO2 by elemental metals in 1-methylimidazole: molecular Cu(CO3)(MeIm)3 and polymeric M(CO3)(MeIm)2·2H2O (M = Co, Zn).Efficient Biomimetic Hydroxylation Catalysis with a Bis(pyrazolyl)imidazolylmethane Copper Peroxide Complex.A family of [Ni8] cages templated by μ6-peroxide from dioxygen activation
P2860
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P2860
Self-assembly of the oxy-tyrosinase core and the fundamental components of phenolic hydroxylation.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh-hant
name
Self-assembly of the oxy-tyros ...... nts of phenolic hydroxylation.
@en
Self-assembly of the oxy-tyros ...... nts of phenolic hydroxylation.
@nl
type
label
Self-assembly of the oxy-tyros ...... nts of phenolic hydroxylation.
@en
Self-assembly of the oxy-tyros ...... nts of phenolic hydroxylation.
@nl
prefLabel
Self-assembly of the oxy-tyros ...... nts of phenolic hydroxylation.
@en
Self-assembly of the oxy-tyros ...... nts of phenolic hydroxylation.
@nl
P2093
P2860
P356
P1433
P1476
Self-assembly of the oxy-tyros ...... nts of phenolic hydroxylation.
@en
P2093
Christopher T Lyons
Cooper Citek
Erik C Wasinger
T Daniel P Stack
P2860
P2888
P304
P356
10.1038/NCHEM.1284
P577
2012-03-04T00:00:00Z