Inhibition of heme peroxidase during phenol derivatives oxidation. Possible molecular cloaking of the active center

Arturas Ziemys, Juozas Kulys

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Ab initio quantum chemical calculations have been applied to the study of the molecular structure of phenol derivatives and oligomers produced during peroxidase-catalyzed oxidation. The interaction of substrates and oligomers with Arthromyces ramosus peroxidase was analyzed by docking methods. The most possible interaction site of oligomers is an active center of the peroxidase. The complexation energy increases with increasing oligomer length. However, the complexed oligomers do not form a precise (for the reaction) hydrogen bonding network in the active center of the enzyme. It seems likely that strong but non productive docking of the oligomers determines peroxidase inhibition during the reaction.

Original languageEnglish (US)
Pages (from-to)245-256
Number of pages12
JournalInternational journal of molecular sciences
Volume6
Issue number9-10
DOIs
StatePublished - 2005

Keywords

  • Ab initio
  • Docking
  • Oligomer
  • Peroxidase
  • Phenol

ASJC Scopus subject areas

  • Chemistry(all)
  • Molecular Biology

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