Glyoxal Oxidase from Phanerochaete chrysosporium Is a New Radical-Copper Oxidase (*)
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Summary
The enzymes represent members of a growing class of free radical metalloenzymes based on the radical-copper catalytic motif and appear to represent functional variants that have evolved to distinct catalytic roles.
- Type
- article
- Published
- 1996-01-12
- Cited by
- 205
- References
- 52
- Access
- Open access
- OpenAlex
- https://openalex.org/W2019222450
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:23118016
Keywords
Phanerochaete, Chrysosporium, Chemistry, Copper, Oxidase test
References
- H2O2 recycling during oxidation of the arylglycerol beta-aryl ether lignin structure by lignin peroxidase and glyoxal oxidase.
- Relationship Between Lignin Degradation and Production of Reduced Oxygen Species by Phanerochaete chrysosporium
- Lignin-Degrading Enzyme from the Hymenomycete Phanerochaete chrysosporium Burds
- Organic chemistry of biological compounds
- Applied molecular genetics of filamentous fungi
- A tyrosine-derived free radical in apogalactose oxidase.
- Re-examination of the products of the action of galactose oxidase. Evidence for the conversion of raffinose to 6''-carboxyraffinose.
- The active site of galactose oxidase.
- Resonance Raman evidence for tyrosine involvement in the radical site of galactose oxidase.
- Galactose oxidase of Dactylium dendroides. Gene cloning and sequence analysis.
- Anion binding to bovine erythrocyte superoxide dismutase. Evidence for multiple binding sites with qualitatively different properties.
- Protein measurement with the Folin phenol reagent.
- Electron Paramagnetic Resonance and Electron Nuclear Double Resonance Spectroscopies of the Radical Site in Galactose Oxidase and of Thioether-Substituted Phenol Model Compounds
- Production and identification of extracellular oxidases of Phanerochaete chrysosporium
- The Reversible Hydration of Carbonyl Compounds in Aqueous Solution. Part I, The Keto/Gem‐diol Equilibrium
- Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase
- Redox activation of galactose oxidase: thin-layer electrochemical study.
- Models for the redox active site in galactose oxidase
- Ultraviolet Resonance Raman Spectroscopy and General Valence Force Field Analysis of Phenolate and Phenoxyl Radical
- Development of Human Neuronal Cell Lines
Cited by
- Phenolate and phenoxyl radical complexes of Cu(II) and Co(III), bearing a new redox active N,O-phenol-pyrazole ligand.
- Shifting redox states of the iron center partitions CDO between crosslink formation or cysteine oxidation.
- Using de novo design proteins to explore tyrosine radicals and cation-π interactions
- Exploring amino-acid radicals and quinone redox chemistry in model proteins
- Conservation of historic timber structures. An ecological approach
- Veratryl alcohol : mechanism of oxidation by lignin peroxidase and role in lignin degradation
- Engineering the substrate specificity of galactose oxidase
- Production and chemiluminescent free radical reactions of glyoxal in lipid peroxidation of linoleic acid by the ligninolytic enzyme, manganese peroxidase.
- Effect of sequestering intrinsic iron on the electron paramagnetic resonance signals in powdered soy proteins.
- A Copper Complex of a Noninnocent Iminophenol-Amidopyridine Hybrid Ligand: Synthesis, Characterization, and Aerobic Alcohol Oxidation
- Posttranslationally modified tyrosines from galactose oxidase and cytochrome c oxidase.
- Copper(I)-phenolate complexes as models of the reduced active site of galactose oxidase: synthesis, characterization, and O2 reactivity
- Structural Studies of Catalysis and Processing in Galactose
- Amine oxidases and galactose oxidase.
- Galactose oxidase: probing radical mechanism with ultrafast radical probe.
- A Small-molecule Model System of Galactose Oxidase: Geometry, Reactivity, and Electronic Structure †‡
- A phenol–imidazole pro-ligand that can exist as a phenoxyl radical, alone and when complexed to copper(II) and zinc(II)
- Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin.
- A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes
- Phenolate and phenoxyl radical complexes of Co(II) and Co(III).
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