Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)

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

doi:10.1016/j.bmcl.2011.03.087

Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)

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

Research output: Contribution to journal › Article › peer-review

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)
Pages (from-to)	2873-2876
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	21
Issue number	10
DOIs	https://doi.org/10.1016/j.bmcl.2011.03.087
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

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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.",

keywords = "Active site modeling, Aminopyrrolnitrin oxygenase (PrnD), Electron transfer, Isc operon, Overexpression",

author = "Tiwari, {Manish Kumar} and Lee, {Jung Kul} and Moon, {Hee Jung} and Huimin Zhao",

note = "Funding Information: This work was supported by the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology ( 331-2007-1-D00144 ) (J.-K.L.), NRF ( 2009-0077718 ) (J.-K.L.), and N00014-02-1-0725 from the US Office of Naval Research (H.Z.). ",

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doi = "10.1016/j.bmcl.2011.03.087",

language = "English (US)",

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AU - Tiwari, Manish Kumar

AU - Lee, Jung Kul

AU - Moon, Hee Jung

AU - Zhao, Huimin

N1 - Funding Information: This work was supported by the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology ( 331-2007-1-D00144 ) (J.-K.L.), NRF ( 2009-0077718 ) (J.-K.L.), and N00014-02-1-0725 from the US Office of Naval Research (H.Z.).

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Y1 - 2011/5/15

N2 - 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.

AB - 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.

KW - Active site modeling

KW - Aminopyrrolnitrin oxygenase (PrnD)

KW - Electron transfer

KW - Isc operon

KW - Overexpression

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