Protein Radicals in Fungal Versatile Peroxidase: CATALYTIC TRYPTOPHAN RADICAL IN BOTH COMPOUND I AND COMPOUND II AND STUDIES ON W164Y, W164H, AND W164S VARIANTS - Wikidata - wikimedia - TriplyDB

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

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

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Crystallographic, Kinetic, and Spectroscopic Study of the First Ligninolytic Peroxidase Presenting a Catalytic Tyrosine Two Oxidation Sites for Low Redox Potential Substrates: A DIRECTED MUTAGENESIS, KINETIC, AND CRYSTALLOGRAPHIC STUDY ON PLEUROTUS ERYNGII VERSATILE PEROXIDASE Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability Demonstration of Lignin-to-Peroxidase Direct Electron Transfer: A TRANSIENT-STATE KINETICS, DIRECTED MUTAGENESIS, EPR, AND NMR STUDY Characterization of three mnp genes of Fomitiporia mediterranea and report of additional class II peroxidases in the order hymenochaetales.Heme enzyme structure and function.Role of surface tryptophan for peroxidase oxidation of nonphenolic lignin Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.Thirty years of heme peroxidase structural biology.Using an artificial tryptophan "wire" in cytochrome c peroxidase for oxidation of organic substrates.The Rise of Radicals in Bioinorganic Chemistry.Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study.The nature of tryptophan radicals involved in the long-range electron transfer of lignin peroxidase and lignin peroxidase-like systems: Insights from quantum mechanical/molecular mechanics simulations.Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: a novel peroxidase activation mechanism.Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques.Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L.Directed evolution of a temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase Prediction of hydrogen-bonding networks around tyrosyl radical inP. eryngiiversatile peroxidase W164Y variants: a QM/MM MD study EPR parameters of amino acid radicals in P. eryngii versatile peroxidase and its W164Y variant computed at the QM/MM level

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P2860

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

http://www.wikidata.org/entity/Q27653485

description

2009 nî lūn-bûn

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2009 թուականի Մարտին հրատարակուած գիտական յօդուած

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2009 թվականի մարտին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Journal of Biological Chemistry

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Protein Radicals in Fungal Ver ...... 64Y, W164H, AND W164S VARIANTS

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Angel T Martínez

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Antonio Romero

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Francisco J Ruiz-Dueñas

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María J Mate

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María Jesús Martínez

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María Morales

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Rebecca Pogni

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Riccardo Basosi

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Stefania Giansanti

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P2860

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

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

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

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

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

Refinement of macromolecular structures by the maximum-likelihood method

The CCP4 suite: programs for protein crystallography

MOLREP: an Automated Program for Molecular Replacement

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

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

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10.1074/JBC.M808069200

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12

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284

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