Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis.
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Cytochrome c/cardiolipin relations in mitochondria: a kiss of deathThe structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substratesCytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA)Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutaseDistal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase: ARGININE BUT NOT ASPARTATE IS ESSENTIAL FOR PEROXIDASE ACTIVITYCrystal structure of horseradish peroxidase C at 2.15 A resolutionEffects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxideHow modification of accessible lysines to phenylalanine modulates the structural and functional properties of horseradish peroxidase: a simulation studyQSAR-assisted design of an environmental catalyst for enhanced estrogen remediation.Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris.Characterization of Dye-decolorizing Peroxidase (DyP) from Thermomonospora curvata Reveals Unique Catalytic Properties of A-type DyPs.Heme enzyme structure and function.Amino acid sequence of anionic peroxidase from the windmill palm tree Trachycarpus fortunei.Peroxidase-type reactions suggest a heterolytic/nucleophilic O-O joining mechanism in the heme-dependent chlorite dismutase.Understanding how the distal environment directs reactivity in chlorite dismutase: spectroscopy and reactivity of Arg183 mutants.Microperoxidase/H2O2-mediated alkoxylating dehalogenation of halophenol derivatives in alcoholic media.Adventures in Rhodococcus - from steroids to explosives.Activation of hydrogen peroxide in horseradish peroxidase occurs within approximately 200 micro s observed by a new freeze-quench device.Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme.Haem propionates control oxidative and reductive activities of horseradish peroxidase by maintaining the correct orientation of the haem.Luffa aegyptiaca (Gourd) Fruit Juice as a Source of Peroxidase.Structural stabilization and functional improvement of horseradish peroxidase upon modification of accessible lysines: experiments and simulation.Reaction of variant sperm-whale myoglobins with hydrogen peroxide: the effects of mutating a histidine residue in the haem distal pocket.Redox- and anion-linked protonation sites in horseradish peroxidase: analysis of distal haem pocket mutants.Expression of the Caldariomyces fumago chloroperoxidase in Aspergillus niger and characterization of the recombinant enzyme.Activity and conformational changes of horseradish peroxidase in trifluoroethanol.Role of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variants.Effects of phthalic anhydride modification on horseradish peroxidase stability and activity.Modified microperoxidases exhibit different reactivity towards phenolic substrates.Crystal structure and functional analysis of Leishmania major pseudoperoxidase.Kinetic characterisation of a dye decolourising peroxidase from Streptomyces lividans: new insight into the mechanism of anthraquinone dye decolourisation.Absence of a detectable intermediate in the compound I formation of horseradish peroxidase at ambient temperature.Spectroscopic and kinetic properties of the horseradish peroxidase mutant T171S. Evidence for selective effects on the reduced state of the enzyme.Spectrophotometric Quantification of Peroxidase with p-Phenylene-diamine for Analyzing Peroxidase-Encapsulating Lipid Vesicles.Glutamic acid-141: a heme 'bodyguard' in anionic tobacco peroxidase.Formation and Decay of Hydroperoxo-Ferric Heme Complex in Horseradish Peroxidase Studied by CryoradiolysisRoles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage
P2860
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P2860
Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Role of arginine 38 in horsera ...... bstrate binding and catalysis.
@en
type
label
Role of arginine 38 in horsera ...... bstrate binding and catalysis.
@en
prefLabel
Role of arginine 38 in horsera ...... bstrate binding and catalysis.
@en
P2093
P2860
P356
P1476
Role of arginine 38 in horsera ...... bstrate binding and catalysis.
@en
P2093
Rodriguez-Lopez JN
Thorneley RN
P2860
P304
P356
10.1074/JBC.271.8.4023
P407
P577
1996-02-01T00:00:00Z