Article Metrics


Online attention

Identification of NAD(P)H quinone oxidoreductase activity in azoreductases from p. aeruginosa: azoreductases and NAD(P)H quinone oxidoreductases belong to the same FMN-dependent superfamily of enzymes

DOI: 10.1371/journal.pone.0098551 DOI Help
PMID: 24915188 PMID Help

Authors: Ali Ryan (University of Oxford) , Elise Kaplan (University of Oxford) , Jean-Christophe Nebel (Kingston University) , Elena Polycarpou (Kingston University) , Vincenzo Crescente (Kingston University) , Ed Lowe (University of Oxford) , Gail M. Preston (University of Oxford) , Edith Sim (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Plos One , VOL 9 (6)

State: Published (Approved)
Published: June 2014

Open Access Open Access

Abstract: Water soluble quinones are a group of cytotoxic anti-bacterial compounds that are secreted by many species of plants, invertebrates, fungi and bacteria. Studies in a number of species have shown the importance of quinones in response to pathogenic bacteria of the genus Pseudomonas. Two electron reduction is an important mechanism of quinone detoxification as it generates the less toxic quinol. In most organisms this reaction is carried out by a group of flavoenzymes known as NAD(P)H quinone oxidoreductases. Azoreductases have previously been separate from this group, however using azoreductases from Pseudomonas aeruginosa we show that they can rapidly reduce quinones. Azoreductases from the same organism are also shown to have distinct substrate specificity profiles allowing them to reduce a wide range of quinones. The azoreductase family is also shown to be more extensive than originally thought, due to the large sequence divergence amongst its members. As both NAD(P)H quinone oxidoreductases and azoreductases have related reaction mechanisms it is proposed that they form an enzyme superfamily. The ubiquitous and diverse nature of azoreductases alongside their broad substrate specificity, indicates they play a wide role in cellular survival under adverse conditions.

Journal Keywords: Quinones; Pseudomonas aeruginosa; Oxidoreductases; Enzyme structure; Oxidation-reduction reactions; Pseudomonas infections; Phylogenetic analysis; Crystal structure

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

Other Facilities: ESRF beamline ID23.2

Added On: 24/02/2015 06:46


Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)