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Akademie Lagerkreis Nautisch galactose oxidase mechanism Becher Vereinfachen Lionel Green Street

Catalytic Galactose Oxidase Models: Biomimetic Cu(II)-Phenoxyl-Radical  Reactivity | Science
Catalytic Galactose Oxidase Models: Biomimetic Cu(II)-Phenoxyl-Radical Reactivity | Science

Sulfanyl stabilization of copper-bonded phenoxyls in model complexes and galactose  oxidase | PNAS
Sulfanyl stabilization of copper-bonded phenoxyls in model complexes and galactose oxidase | PNAS

Galactose oxidase - Wikipedia
Galactose oxidase - Wikipedia

Galactose oxidase - Wikipedia
Galactose oxidase - Wikipedia

Preparation of galactose oxidase functional phosphorescent quantum dots and  detection of D-galactose.,Spectrochimica Acta Part A: Molecular and  Biomolecular Spectroscopy - X-MOL
Preparation of galactose oxidase functional phosphorescent quantum dots and detection of D-galactose.,Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - X-MOL

Galactose oxidase | owlapps
Galactose oxidase | owlapps

M-CSA Mechanism and Catalytic Site Atlas
M-CSA Mechanism and Catalytic Site Atlas

Cu( ii )-nitroxyl radicals as catalytic galactose oxidase mimics - Organic  & Biomolecular Chemistry (RSC Publishing) DOI:10.1039/B305941C
Cu( ii )-nitroxyl radicals as catalytic galactose oxidase mimics - Organic & Biomolecular Chemistry (RSC Publishing) DOI:10.1039/B305941C

Cu(I)-dependent Biogenesis of the Galactose Oxidase Redox Cofactor* -  Journal of Biological Chemistry
Cu(I)-dependent Biogenesis of the Galactose Oxidase Redox Cofactor* - Journal of Biological Chemistry

Galactose oxidase - Alchetron, The Free Social Encyclopedia
Galactose oxidase - Alchetron, The Free Social Encyclopedia

Galactose oxidase - Wikiwand
Galactose oxidase - Wikiwand

Galactose oxidase - Wikiwand
Galactose oxidase - Wikiwand

Galactose Oxidase - an overview | ScienceDirect Topics
Galactose Oxidase - an overview | ScienceDirect Topics

Galactose Oxidase - Worthington Enzyme Manual
Galactose Oxidase - Worthington Enzyme Manual

Catalytic Promiscuity of Galactose Oxidase: A Mild Synthesis of Nitriles  from Alcohols, Air, and Ammonia - Vilím - 2018 - Angewandte Chemie - Wiley  Online Library
Catalytic Promiscuity of Galactose Oxidase: A Mild Synthesis of Nitriles from Alcohols, Air, and Ammonia - Vilím - 2018 - Angewandte Chemie - Wiley Online Library

Homemade cofactors: Self-processing in galactose oxidase | PNAS
Homemade cofactors: Self-processing in galactose oxidase | PNAS

Recent Advances in One‐Electron‐Oxidized CuII–Diphenoxide Complexes as  Models of Galactose Oxidase: Importance of the Structural Flexibility in  the Active Site - Oshita - 2020 - Chemistry – A European Journal - Wiley  Online Library
Recent Advances in One‐Electron‐Oxidized CuII–Diphenoxide Complexes as Models of Galactose Oxidase: Importance of the Structural Flexibility in the Active Site - Oshita - 2020 - Chemistry – A European Journal - Wiley Online Library

M-CSA Mechanism and Catalytic Site Atlas
M-CSA Mechanism and Catalytic Site Atlas

Galactose Oxidase - Creative Enzymes
Galactose Oxidase - Creative Enzymes

Molecules | Free Full-Text | Co-Immobilization of Tri-Enzymes for the  Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran | HTML
Molecules | Free Full-Text | Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran | HTML

Redox active ligand and metal cooperation for C(sp2)–H oxidation: extension  of the galactose oxidase mechanism in water-mediated amide formation -  Dalton Transactions (RSC Publishing)
Redox active ligand and metal cooperation for C(sp2)–H oxidation: extension of the galactose oxidase mechanism in water-mediated amide formation - Dalton Transactions (RSC Publishing)

Aerobic oxidation of alcohol by model complexes relevant to metal site galactose  oxidase: role of copper(I) intermediate, evidence for the generation of  end-on copper(II)–OOH species and catalytic promiscuity for oxidation of  benzyl
Aerobic oxidation of alcohol by model complexes relevant to metal site galactose oxidase: role of copper(I) intermediate, evidence for the generation of end-on copper(II)–OOH species and catalytic promiscuity for oxidation of benzyl