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Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)
Authors:Tiwari Manish Kumar  Lee Jung-Kul  Moon Hee-Jung  Zhao Huimin
Affiliation:a Department of Chemical Engineering, Konkuk University, Seoul 143-701, Republic of Korea
b Department of Chemical and Biomolecular Engineering, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, United States
c Department of Chemistry, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, United States
d Department of Bioengineering, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, United States
e Institute for Genomic Biology, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, United States
f Center for Biophysics and Computational Biology, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, United States
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.
Keywords:Aminopyrrolnitrin oxygenase (PrnD)   Active site modeling   Electron transfer   Isc operon   Overexpression
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