(Q71973423)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

title

Effect of distal cavity mutations on the binding and activation of oxygen by ferrous horseradish peroxidase (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

José Neptuno Rodríguez-López

22 October 2019

author

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

author name string

A T Smith

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

R N Thorneley

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

language of work or name

English

0 references

publication date

1 January 1997

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

22 October 2019

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

volume

272

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

issue

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

page(s)

389-395

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

Superfamily of plant, fungal and bacterial peroxidases

22 October 2019

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Reactions of the oxyform of horseradish peroxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

The kinetics of oxidation of ferroperoxidase by molecular oxygen. A model of a terminal oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Reaction of ferrous cytochrome c peroxidase with dioxygen: site-directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound I radical site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Amino-acid sequences of heme-linked, histidine-containing peptides of five peroxidases from horseradish and turnip

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41 Val, with altered reactivity towards hydrogen peroxide and reducing substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Laser Photolysis Behavior of Ferrous Horseradish Peroxidase with Carbon Monoxide and Cyanide: Effects of Mutations in the Distal Heme Pocket

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Perturbations of the distal heme pocket in human myoglobin mutants probed by infrared spectroscopy of bound CO: correlation with ligand binding kinetics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Interactions among residues CD3, E7, E10, and E11 in myoglobins: attempts to simulate the ligand-binding properties of Aplysia myoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Kinetics of oxygen and carbon monoxide binding to the hemoglobins of Glycera dibranchiata

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Resonance Raman spectroscopic characterization of compound III of lignin peroxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Crystallization and preliminary X-ray studies of recombinant horseradish peroxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Characterization of recombinant horseradish peroxidase C and three site-directed mutants, F41V, F41W, and R38K, by resonance Raman spectroscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Structure of hemoglobins Zürich [His E7(63)beta replaced by Arg] and Sydney [Val E11(67)beta replaced by Ala] and role of the distal residues in ligand binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Elementary steps in the formation of horseradish peroxidase compound I: direct observation of compound 0, a new intermediate with a hyperporphyrin spectrum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

Mechanism of indole-3-acetic acid oxidation by plant peroxidases: anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.1.389

21 January 2018

Identifiers

DOI

10.1074/JBC.272.1.389

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8995273%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

1 reference