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Biologically inspired oxidation catalysis
scientific article published on September 2008
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scholarly article
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Europe PubMed Central
PubMed ID
18800132
retrieved
19 August 2017
review article
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Europe PubMed Central
title
Biologically inspired oxidation catalysis
(English)
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Europe PubMed Central
PubMed ID
18800132
retrieved
19 August 2017
author name string
Lawrence Que
series ordinal
1
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Europe PubMed Central
PubMed ID
18800132
retrieved
19 August 2017
William B Tolman
series ordinal
2
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Europe PubMed Central
PubMed ID
18800132
retrieved
19 August 2017
language of work or name
English
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publication date
1 September 2008
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Europe PubMed Central
PubMed ID
18800132
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19 August 2017
number of pages
8
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published in
Nature
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Europe PubMed Central
PubMed ID
18800132
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19 August 2017
volume
455
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Europe PubMed Central
PubMed ID
18800132
retrieved
19 August 2017
page(s)
333-340
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Europe PubMed Central
PubMed ID
18800132
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19 August 2017
issue
7211
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Europe PubMed Central
PubMed ID
18800132
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19 August 2017
exact match
https://scigraph.springernature.com/pub.10.1038/nature07371
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Catalysis research of relevance to carbon management: progress, challenges, and opportunities.
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Recent advances in transition metal catalyzed oxidation of organic substrates with molecular oxygen
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Biomimetic modeling of copper oxidase reactivity
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Green Chemistry and Catalysis
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Structure and chemistry of cytochrome P450.
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Probing Structure-Function Relations in Heme-Containing Oxygenases and Peroxidases
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Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins
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Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers
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Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters
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An Fe2IVO2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase
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Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron
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Non-heme Fe(IV)-oxo intermediates
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Oxygen Binding, Activation, and Reduction to Water by Copper Proteins
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Free radical catalysis by galactose oxidase
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Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase
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The Stacking Tryptophan of Galactose Oxidase: A Second-Coordination Sphere Residue that Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis † , ‡
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Systematic development of computational models for the catalytic site in galactose oxidase: impact of outer-sphere residues on the geometric and electronic structures.
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Crossref
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Catalytic reaction profile for alcohol oxidation by galactose oxidase
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Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin
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Mechanistic insight into the activity of tyrosinase from variable-temperature studies in an aqueous/organic solvent.
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Structure and spectroscopy of copper-dioxygen complexes.
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Tyrosinase reactivity in a model complex: an alternative hydroxylation mechanism.
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The copper-enzyme family of dopamine beta-monooxygenase and peptidylglycine alpha-hydroxylating monooxygenase: resolving the chemical pathway for substrate hydroxylation
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Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species.
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1 reference
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1 reference
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inferred from DOI database lookup
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1 reference
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1 reference
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1 reference
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inferred from DOI database lookup
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1 reference
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7 January 2021
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Identifiers
DOI
10.1038/NATURE07371
1 reference
stated in
Europe PubMed Central
PubMed ID
18800132
retrieved
19 August 2017
PubMed ID
18800132
1 reference
stated in
Europe PubMed Central
PubMed ID
18800132
retrieved
19 August 2017
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