Protein Radicals in Fungal Versatile Peroxidase: CATALYTIC TRYPTOPHAN RADICAL IN BOTH COMPOUND I AND COMPOUND II AND STUDIES ON W164Y, W164H, AND W164S VARIANTS (Q27653485)

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English	Protein Radicals in Fungal Versatile Peroxidase: CATALYTIC TRYPTOPHAN RADICAL IN BOTH COMPOUND I AND COMPOUND II AND STUDIES ON W164Y, W164H, AND W164S VARIANTS	scientific article

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scholarly article

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Protein Radicals in Fungal Versatile Peroxidase: CATALYTIC TRYPTOPHAN RADICAL IN BOTH COMPOUND I AND COMPOUND II AND STUDIES ON W164Y, W164H, AND W164S VARIANTS (English)

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author name string

Francisco J Ruiz-Dueñas

1

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Rebecca Pogni

2

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María Morales

3

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Stefania Giansanti

4

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María J Mate

5

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Antonio Romero

6

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María Jesús Martínez

7

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Riccardo Basosi

8

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Angel T Martínez

9

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language of work or name

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publication date

20 March 2009

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Journal of Biological Chemistry

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284

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12

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7986-94

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Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase

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MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

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Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism

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The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle

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Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c

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Refinement of macromolecular structures by the maximum-likelihood method

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Microbial degradation of lignin: how a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of this

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Role of fungal peroxidases in biological ligninolysis.

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Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium

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29 September 2017

Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways.

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Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin.

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Structure and interactions of amino acid radicals in class I ribonucleotide reductase studied by ENDOR and high-field EPR spectroscopy

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29 September 2017

Molecular dynamics simulations of lignin peroxidase in solution

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29 September 2017

Sensitivity of tyrosyl radical g-values to changes in protein structure: a high-field EPR study of mutants of ribonucleotide reductase.

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29 September 2017

Oxidation of a tetrameric nonphenolic lignin model compound by lignin peroxidase.

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29 September 2017

Manganese peroxidase

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29 September 2017

Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans

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Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites

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29 September 2017

Direct interaction of lignin and lignin peroxidase from Phanerochaete chrysosporium

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29 September 2017

Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii.

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29 September 2017

Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis

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29 September 2017

Enzymatic "combustion": the microbial degradation of lignin

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29 September 2017

Horseradish peroxidase compound I: evidence for spin coupling between the heme iron and a ‘free’ radical

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29 September 2017

Substrate binding and catalysis in heme peroxidases.

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2 June 2018

Tryptophan-based radical in the catalytic mechanism of versatile peroxidase from Bjerkandera adusta

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21 January 2018

A tryptophan neutral radical in the oxidized state of versatile peroxidase from Pleurotus eryngii: a combined multifrequency EPR and density functional theory study.

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21 January 2018

Lignin peroxidase oxidation of veratryl alcohol: effects of the mutants H82A, Q222A, W171A, and F267L.

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21 January 2018

Protein-based radicals in the catalase-peroxidase of synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site

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21 January 2018

Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: potential oxidation sites for oxidative polymerization of lignin

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21 January 2018

MOLREP: an Automated Program for Molecular Replacement

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21 January 2018

Tyrosine radical formation in the reaction of wild type and mutant cytochrome P450cam with peroxy acids: a multifrequency EPR study of intermediates on the millisecond time scale

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21 January 2018

Tryptophan and tyrosine radicals in ribonucleotide reductase: a comparative high-field EPR study at 94 GHz.

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21 January 2018

Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes

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21 January 2018

Identification of the myoglobin tyrosyl radical by immuno-spin trapping and its dimerization

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21 January 2018

EPR and ENDOR detection of compound I from Micrococcus lysodeikticus catalase

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12 December 2020

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EPR investigation of compound I in Proteus mirabilis and bovine liver catalases: formation of porphyrin and tyrosyl radical intermediates

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https://pubmed.ncbi.nlm.nih.gov/19158088

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Evidence from spin-trapping for a transient radical on tryptophan residue 171 of lignin peroxidase

1 reference

https://pubmed.ncbi.nlm.nih.gov/19158088

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Do carbohydrates play a role in the lignin peroxidase cycle? Redox catalysis in the endergonic region of the driving force

1 reference

https://pubmed.ncbi.nlm.nih.gov/19158088

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein Radicals in Enzyme Catalysis

1 reference

https://pubmed.ncbi.nlm.nih.gov/19158088

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Electron-tunneling pathways in proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/19158088

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Control of the transfer of oxidizing equivalents between heme iron and free radical site in yeast cytochrome c peroxidase

1 reference

https://pubmed.ncbi.nlm.nih.gov/19158088

12 December 2020

based on heuristic

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Manganese Oxidation Site inPleurotus eryngiiVersatile Peroxidase: A Site-Directed Mutagenesis, Kinetic, and Crystallographic Study†,‡

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M808069200

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release_szaovhhlvnfozgt4kmar3dsnoe

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