Peroxidase-type reactions suggest a heterolytic/nucleophilic O-O joining mechanism in the heme-dependent chlorite dismutase (Q35323100)

7 August 2017

title

Peroxidase-type reactions suggest a heterolytic/nucleophilic O-O joining mechanism in the heme-dependent chlorite dismutase (English)

1 reference

7 August 2017

author

Gudrun S Lukat-Rodgers

4

object named as

Gudrun S Lukat-Rodgers

1 reference

7 August 2017

Jeffrey A Mayfield

1

1 reference

7 August 2017

Béatrice Blanc

2

1 reference

7 August 2017

Kenton R Rodgers

3

1 reference

7 August 2017

Jennifer L DuBois

5

1 reference

7 August 2017

language of work or name

English

0 references

publication date

23 September 2013

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7 August 2017

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7 August 2017

volume

52

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7 August 2017

issue

40

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7 August 2017

page(s)

6982-6994

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Understanding the roles of strictly conserved tryptophan residues in O2 producing chlorite dismutases

7 August 2017

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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Mechanism of the chlorination reaction catalyzed by horseradish peroxidase with chlorite

12 July 2018

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Kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength

12 July 2018

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12 July 2018

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26 September 2018

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26 September 2018

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26 September 2018

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26 September 2018

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12 December 2020

Ligand binding and structural perturbations in cytochrome c peroxidase. A crystallographic study

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12 December 2020

Inactivation of peroxidase by hydrogen peroxide and its protection by a reductant agent

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Role of distal arginine in early sensing intermediates in the heme domain of the oxygen sensor FixL

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Electronic design criteria for O-O bond formation via metal-oxo complexes

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Mechanism of reaction of horseradish peroxidase with chlorite and chlorine dioxide

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The reaction of chloroperoxidase with chlorite and chlorine dioxide

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YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins

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The inactivation and catalytic pathways of horseradish peroxidase with m-chloroperoxybenzoic acid. A spectrophotometric and transient kinetic study

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Identifiers

DOI

10.1021/BI4005599

1 reference

7 August 2017

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7 August 2017

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