title: Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD).
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.
authors.affiliation: Department of Chemical Engineering, Konkuk University, Seoul 143-701, Republic of Korea.
authors.forename: Manish Kumar
authors.initials: MK
authors.lastname: Tiwari
authors.forename: Jung-Kul
authors.initials: JK
authors.lastname: Lee
authors.forename: Hee-Jung
authors.initials: HJ
authors.lastname: Moon
authors.forename: Huimin
authors.initials: H
authors.lastname: Zhao
mesh_terms: D000588:Amines / Q000737:chemistry*; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010105:Oxygenases / Q000737:chemistry* / Q000235:genetics; D011764:Pyrrolnitrin / Q000737:chemistry*
chemical_list: D000588:Amines; D010105:Oxygenases; D011764:Pyrrolnitrin