(Q27622235)

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X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution

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X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution (English)

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T J Fiedler

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C A Davey

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R E Fenna

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language of work or name

English

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publication date

21 April 2000

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published in

Journal of Biological Chemistry

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volume

275

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issue

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page(s)

11964-71

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cites work

The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase

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21 January 2018

Myeloperoxidase: contribution to the microbicidal activity of intact leukocytes.

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21 January 2018

Peroxidase-mediated virucidal systems

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21 January 2018

Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionarily related members of the same gene family

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21 January 2018

Primary structure of bovine lactoperoxidase, a fourth member of a mammalian heme peroxidase family

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21 January 2018

X-ray crystal structure of canine myeloperoxidase at 3 A resolution

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21 January 2018

The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1

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21 January 2018

Structure of the green heme in myeloperoxidase

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21 January 2018

Compounds I of catalase and horse radish peroxidase: pi-cation radicals

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21 January 2018

Myeloperoxidase of human neutrophilic granulocytes as chlorinating enzyme.

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21 January 2018

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

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21 January 2018

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.275.16.11964

retrieved

21 January 2018

Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species

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reference URL

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retrieved

21 January 2018

Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group.

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.275.16.11964

retrieved

21 January 2018

Site-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction

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https://api.crossref.org/works/10.1074%2FJBC.275.16.11964

retrieved

21 January 2018

Detection of an oxyferryl porphyrin pi-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I.

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.275.16.11964

retrieved

21 January 2018

Identifiers

DOI

10.1074/JBC.275.16.11964

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

819169

OpenCitations bibliographic resource ID

819169

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

819169

PubMed publication ID

10766826

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

819169

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