Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase
about
Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system.Dioxygen activation in soluble methane monooxygenaseInsights into the different dioxygen activation pathways of methane and toluene monooxygenase hydroxylasesCharacterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy.Structural, EPR, and Mössbauer characterization of (μ-alkoxo)(μ-carboxylato)diiron(II,III) model complexes for the active sites of mixed-valent diiron enzymes.Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes.Time-Resolved Investigations of Heterobimetallic Cofactor Assembly in R2lox Reveal Distinct Mn/Fe Intermediates.Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway.A Carboxylate Shift Regulates Dioxygen Activation by the Diiron Nonheme β-Hydroxylase CmlA upon Binding of a Substrate-Loaded Nonribosomal Peptide Synthetase.New mechanistic insights into intramolecular aromatic ligand hydroxylation and benzyl alcohol oxidation initiated by the well-defined (μ-peroxo)diiron(iii) complex.In-crystal reaction cycle of a toluene-bound diiron hydroxylase.New mechanistic insight into intramolecular arene hydroxylation initiated by (μ-1,2-peroxo)diiron(III) complexes with dinucleating ligands.A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation.Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI.Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Cavity residue leucine 95 and channel residues glutamine 204, aspartic acid 211, and phenylalanine 269 of toluene o-xylene monooxygenase influence catalysis.Diiron monooxygenases in natural product biosynthesis.Roles of carboxylate donors in O–O bond scission of peroxodi-iron(iii) to high-spin oxodi-iron(iv) with a new carboxylate-containing dinucleating ligand
P2860
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P2860
Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase
description
2009 nî lūn-bûn
@nan
2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Crystallographic and catalytic ...... action in a diiron hydroxylase
@ast
Crystallographic and catalytic ...... action in a diiron hydroxylase
@en
Crystallographic and catalytic ...... action in a diiron hydroxylase
@nl
type
label
Crystallographic and catalytic ...... action in a diiron hydroxylase
@ast
Crystallographic and catalytic ...... action in a diiron hydroxylase
@en
Crystallographic and catalytic ...... action in a diiron hydroxylase
@nl
prefLabel
Crystallographic and catalytic ...... action in a diiron hydroxylase
@ast
Crystallographic and catalytic ...... action in a diiron hydroxylase
@en
Crystallographic and catalytic ...... action in a diiron hydroxylase
@nl
P356
P1433
P1476
Crystallographic and catalytic ...... action in a diiron hydroxylase
@en
P2093
Brian G Fox
Lucas J Bailey
P304
P356
10.1021/BI901150A
P407
P577
2009-09-29T00:00:00Z