Work

Structural Insight into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases

Year: 2012

Type: article

Abstract: SidA from the human pathogen Aspergillus fumigatus catalyzes the generation of N(5)-hydroxyornithine in the biosynthesis of siderophores, a reaction essential for virulence. The crystal structures of SidA in complex with ornithine and lysine reveal the geometry of the interactions among flavin, NADP(+), and the substrate amine group that underlie the hydroxylation reaction. The structural elucidation of the enzyme in complex with arginine provides insight into the role of electrostatics and hydrogen bonding in the mechanism of oxygen activation in this family of enzymes.

Source: Biochemistry

DOI: 10.1021/bi301072w

Authors: Stefano Franceschini, Michael Fedkenheuer, Nancy J. Vogelaar, Howard H. Robinson, Pablo Sobrado, Andrea Mattevi

Institutions: University of Pavia, Virginia Tech, Brookhaven National Laboratory

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: bronze

Funders: National Science Foundation, Fondazione Cariplo

Award: Mechanistic and Structural Studies of Flavin Dependent N-hydroxylating Monooxygenases