The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme
about
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolutionUnusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidaseCytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA)Replacement of an Electron Transfer Pathway in Cytochrome c Peroxidase with a Surrogate Peptide † , ‡Ultrahigh (0.93Å) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: Implications for the catalytic mechanismStructural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutaseStructure of dehaloperoxidase B at 1.58 Å resolution and structural characterization of the AB dimer fromAmphitrite ornataInternal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase FunctionCrystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157Crystal Structure of Leishmania major Peroxidase and Characterization of the Compound I Tryptophan RadicalStructure of a bacterial cell surface decaheme electron conduitMutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesisConstruction of a bisaquo heme enzyme and binding by exogenous ligandsCrystal structures of substrate binding site mutants of manganese peroxidaseReduction potential of yeast cytochrome c peroxidase and three distal histidine mutants: dependence on pHPeroxidase-Catalyzed Oxidation of Ascorbate Structural, Spectroscopic and Mechanistic Correlations in Ascorbate PeroxidaseNoncovalent self-assembly of a heterotetrameric diiron protein.Trapping of peptide-based surrogates in an artificially created channel of cytochrome c peroxidase.DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases.Binding and docking interactions of NO, CO and O₂in heme proteins as probed by density functional theoryLegionella pneumophila catalase-peroxidases: cloning of the katB gene and studies of KatB functionFlavohemoglobin, a globin with a peroxidase-like catalytic site.Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulum.Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology.Peroxidase activity and involvement in the oxidative stress response of roseobacter denitrificans truncated hemoglobin.Effect of active site and surface mutations on the reduction potential of yeast cytochrome c peroxidase and spectroscopic properties of the oxidized and reduced enzyme.The role of aspartate-235 in the binding of cations to an artificial cavity at the radical site of cytochrome c peroxidase.Protein conformer selection by ligand binding observed with crystallography.Geometric and electronic structures of the His-Fe(IV)=O and His-Fe(IV)-Tyr hemes of MauG.Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Impact of Proximal and Distal Pocket Site-Directed Mutations on the Ferric/Ferrous Heme Redox Potential of Yeast Cytochrome-c-PeroxidaseEffects of imidazole deprotonation on vibrational spectra of high-spin iron(II) porphyrinates.Heme attachment motif mobility tunes cytochrome c redox potentialReplacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization.Tyrosyl radicals in dehaloperoxidase: how nature deals with evolving an oxygen-binding globin to a biologically relevant peroxidase.Exploring the biochemistry at the extracellular redox frontier of bacterial mineral Fe(III) respiration.Peroxygenase reactions catalyzed by cytochromes P450.Functional consequences of the creation of an Asp-His-Fe triad in a 3/3 globin.Mapping quantitative trait loci for peroxidase activity and developing gene-specific markers for TaPod-A1 on wheat chromosome 3AL.Active site of cytochrome cbb3.
P2860
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P2860
The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme
description
1993 nî lūn-bûn
@nan
1993 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@ast
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@en
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@nl
type
label
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@ast
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@en
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@nl
prefLabel
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@ast
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@en
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@nl
P356
P1433
P1476
The Asp-His-Fe triad of cytoch ...... ophan free radical to the heme
@en
P2093
P304
P356
10.1021/BI00064A014
P407
P577
1993-04-06T00:00:00Z