Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)

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

Research output: Contribution to journalArticlepeer-review


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
Issue number10
StatePublished - May 15 2011


  • 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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