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 language | English (US) |
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Pages (from-to) | 2873-2876 |
Number of pages | 4 |
Journal | Bioorganic and Medicinal Chemistry Letters |
Volume | 21 |
Issue number | 10 |
DOIs | |
State | Published - 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