Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.
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.
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PA1204 is discussed as a putative azoreductase by structural homology; its quinone reductase activity is cited from other work (reference 75), not assayed here.
"Recent data have shown that PA0949, PA1204, PA2580 and PA4975, have NAD(P)H quinone oxidoreductase activities [75]."
Pseudomonas aeruginosa MdaB and WrbA are water-soluble two-electron quinone oxidoreductases with the potential to defend against oxidative stress.
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Five P. aeruginosa quinone oxidoreductase orthologs reduce quinones in vitro by a two-electron route.
"In in vitro assays, each enzyme was shown to reduce quinone substrates with only minimal semiquinone formation."
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Only WrbA and MdaB overexpression protected a katA mutant against H2O2.
"in a katA mutant, H2O2 challenged strains over-expressing the WrbA and MdaB orthologs grew significantly better than the empty plasmid control"