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A role of proton transfer in peroxidase-catalyzed process elucidated by substrates docking calculations

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A role of proton transfer in peroxidase-catalyzed process elucidated by substrates docking calculations (English)

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J Kulys

1

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A Ziemys

series ordinal

2

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language of work or name

English

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publication date

2001

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published in

BMC Structural Biology

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volume

1

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issue

1

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page(s)

3

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cites work

The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55340

retrieved

7 April 2017

Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X-ray crystallographic analysis of the complex at 1.6 A resolution

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55340

retrieved

7 April 2017

Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 A resolution. Structural comparisons with the lignin and cytochrome c peroxidases

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=55340

retrieved

7 April 2017

Kinetics and thermodynamics of peroxidase- and laccase-catalyzed oxidation of N-substituted phenothiazines and phenoxazines

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11545682

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12 December 2020

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inferred from PubMed ID database lookup

Roles of water in heme peroxidase and catalase mechanisms

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11545682

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12 December 2020

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Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11545682

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Factors controlling the substrate specificity of peroxidases: kinetics and thermodynamics of the reaction of horseradish peroxidase compound I with phenols and indole-3-acetic acids

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11545682

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12 December 2020

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

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11545682

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12 December 2020

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DOI

10.1186/1472-6807-1-3

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Dimensions Publication ID

1038385101

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PMC publication ID

55340

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PubMed publication ID

11545682

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ResearchGate publication ID

11800966

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(Q24804073)

A role of proton transfer in peroxidase-catalyzed process elucidated by substrates docking calculations

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