Crystal structure of horseradish peroxidase C at 2.15 A resolution (Q27748751)

https://api.crossref.org/works/10.1038/NSB1297-1032

SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

20 April 2017

1 reference

https://api.crossref.org/works/10.1038/NSB1297-1032

VMD: visual molecular dynamics

20 April 2017

1 reference

https://api.crossref.org/works/10.1038/NSB1297-1032

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

20 April 2017

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Rates of reaction of indoleacetic acids with horseradish peroxidase compound I and their dependence on the redox potentials.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Horseradish peroxidase His-42 --> Ala, His-42 --> Val, and Phe-41 --> Ala mutants. Histidine catalysis and control of substrate access to the heme iron

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Rescue of His-42 --> Ala horseradish peroxidase by a Phe-41 --> His mutation. Engineering of a surrogate catalytic histidine

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Rescue of the horseradish peroxidase His-170-->Ala mutant activity by imidazole: importance of proximal ligand tethering

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Refinement of 3D models of horseradish peroxidase isoenzyme C: predictions of 2D NMR assignments and substrate binding sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

[25] Protein multiple sequence alignment and flexible pattern matching

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

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/10.1038%2FNSB1297-1032

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Kinetic and molecular orbital studies on the rate of oxidation of monosubstituted phenols and anilines by horseradish peroxidase compound II.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Two-dimensional 1H-NMR studies of horseradish peroxidase C and its interaction with indole-3-propionic acid

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Solution Characterisation by NMR Spectroscopy of Two Horseradish Peroxidase Isoenzyme C Mutants with Alanine Replacing Either Phe142 or Phe143

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

The use of methyl-substituted benzhydroxamic acids as structural probes of peroxidase substrate binding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Catalytic Sites of Hemoprotein Peroxidases

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Baculovirus expression and characterization of catalytically active horseradish peroxidase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Catalytic roles of the distal site asparagine-histidine couple in peroxidases

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Mutation of Distal Residues of Horseradish Peroxidase: Influence on Substrate Binding and Cavity Properties†

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

The crystal structure of peanut peroxidase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Crystal structure of recombinant pea cytosolic ascorbate peroxidase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Improved methods for building protein models in electron density maps and the location of errors in these models

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Amino Acid Sequence Studies of Horseradish Peroxidase. Amino and Carboxyl Termini, Cyanogen Bromide and Tryptic Fragments, the Complete Sequence, and Some Structural Characteristics of Horseradish Peroxidase C

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

A comparative study of the inactivation of wild-type, recombinant and two mutant horseradish peroxidase isoenzymes C by hydrogen peroxide and m-chloroperoxybenzoic acid.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Resonance Raman investigation of ferric iron in horseradish peroxidase and its aromatic donor complexes at room and low temperatures

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

A step towards understanding the folding mechanism of horseradish peroxidase. Tryptophan fluorescence and circular dichroism equilibrium studies

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Structural studies by proton-NMR spectroscopy of plant horseradish peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41----Val and Arg38----Lys

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Identification of a porphyrin pi cation radical in ascorbate peroxidase compound I.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Identification of a critical phenylalanine residue in horseradish peroxidase, Phe179, by site-directed mutagenesis and 1H-NMR: implications for complex formation with aromatic donor molecules

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Comparison of structure and activities of peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Unit cell dimensions of crystalline horseradish peroxidase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

The study of intact proteins and glycoproteins by electrospray m.s

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

AMoRe: an automated package for molecular replacement

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Solvent content of protein crystals

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Accurate bond and angle parameters for X-ray protein structure refinement

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032

ALSCRIPT: a tool to format multiple sequence alignments

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSB1297-1032