Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)

Manish Kumar Tiwari, Jung Kul Lee, Hee Jung Moon, Huimin Zhao

Research output: Contribution to journalArticle

Abstract

Active site modeling of dimerization interface in combination with site-directed mutagenesis indicates that the electron in the PrnD Rieske oxygenase can be transferred by either of two pathways, one involving Asp183′ and the other involving Asn180′. In addition, the overexpression of the isc operon involved in the assembly of iron-sulfur clusters increased the catalytic activity of PrnD in Escherichia coli by a factor of at least 4.

Original languageEnglish (US)
Pages (from-to)2873-2876
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume21
Issue number10
DOIs
StatePublished - May 15 2011

Keywords

  • Active site modeling
  • Aminopyrrolnitrin oxygenase (PrnD)
  • Electron transfer
  • Isc operon
  • Overexpression

ASJC Scopus subject areas

  • Pharmaceutical Science
  • Drug Discovery
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry
  • Biochemistry

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