Reconstitution and Characterization of Aminopyrrolnitrin Oxygenase, a Rieske N-Oxygenase That Catalyzes Unusual Arylamine Oxidation

Lee, Jung-Kul; Simurdiak, Michael; Zhao, Huimin

doi:10.1074/jbc.m505334200

Cited by 88 publications

(91 citation statements)

References 65 publications

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“…The best-characterized examples of N-oxygenases are from the biosynthesis of pyrrolnitrin and aureothin. The multicomponent oxygenase PrnD from Pseudomonas fluorescens catalyzes the conversion of aminopyrrolnitrin to pyrrolnitrin by using molecular oxygen as the substrate (63,99,104). Biochemical characterization confirmed bioinformatic predictions that PrnD is indeed a Rieske-type oxygenase that uses NAD(P)H and flavin as electron donors.…”

Section: Naturally Occurring Nitroaromatic Compoundsmentioning

confidence: 70%

Nitroaromatic Compounds, from Synthesis to Biodegradation

Parales

2010

Microbiol Mol Biol Rev

775

470

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SUMMARY Nitroaromatic compounds are relatively rare in nature and have been introduced into the environment mainly by human activities. This important class of industrial chemicals is widely used in the synthesis of many diverse products, including dyes, polymers, pesticides, and explosives. Unfortunately, their extensive use has led to environmental contamination of soil and groundwater. The nitro group, which provides chemical and functional diversity in these molecules, also contributes to the recalcitrance of these compounds to biodegradation. The electron-withdrawing nature of the nitro group, in concert with the stability of the benzene ring, makes nitroaromatic compounds resistant to oxidative degradation. Recalcitrance is further compounded by their acute toxicity, mutagenicity, and easy reduction into carcinogenic aromatic amines. Nitroaromatic compounds are hazardous to human health and are registered on the U.S. Environmental Protection Agency's list of priority pollutants for environmental remediation. Although the majority of these compounds are synthetic in nature, microorganisms in contaminated environments have rapidly adapted to their presence by evolving new biodegradation pathways that take advantage of them as sources of carbon, nitrogen, and energy. This review provides an overview of the synthesis of both man-made and biogenic nitroaromatic compounds, the bacteria that have been identified to grow on and completely mineralize nitroaromatic compounds, and the pathways that are present in these strains. The possible evolutionary origins of the newly evolved pathways are also discussed.

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Section: Naturally Occurring Nitroaromatic Compoundsmentioning

confidence: 70%

Nitroaromatic Compounds, from Synthesis to Biodegradation

Parales

2010

Microbiol Mol Biol Rev

775

470

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“…A romatic nitro groups are relatively rare functional groups in natural products but are found in diverse types of important antibiotics, such as chloramphenicol, pyrrolnitrin, aureothin, azomycin, and rufomycin (1)(2)(3). The biosynthesis of aromatic nitro groups is poorly understood.…”

Section: Di-iron Enzymes ͉ Metalloenzymes ͉ N-oxygenation ͉ Reaction mentioning

confidence: 99%

“…One is p-nitrobenzoate N-oxygenase (AurF) involved in the biosynthesis of aureothin (4). The other, aminopyrrolnitrin N-oxygenase (PrnD), a Rieske mononuclear non-heme iron enzyme involved in the biosynthesis of pyrrolnitrin, catalyzes the conversion of aminopyrrolnitrin to pyrrolnitrin (3,5). Notably, AurF shares no sequence homology with any other functionally characterized oxygenases in the Swiss-Prot database, and the purified enzyme did not show any native enzymatic activity (6,7), although a ''peroxide shunt'' was recently found to be able to restore the enzymatic activity (8).…”

Section: Di-iron Enzymes ͉ Metalloenzymes ͉ N-oxygenation ͉ Reaction mentioning

confidence: 99%

In vitro reconstitution and crystal structure of p -aminobenzoate N -oxygenase (AurF) involved in aureothin biosynthesis

Choi¹,

Zhang

Brunzelle

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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150

216

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p-aminobenzoate N-oxygenase (AurF) from Streptomyces thioluteus catalyzes the formation of unusual polyketide synthase starter unit p-nitrobenzoic acid (pNBA) from p-aminobenzoic acid (pABA) in the biosynthesis of antibiotic aureothin. AurF is a metalloenzyme, but its native enzymatic activity has not been demonstrated in vitro, and its catalytic mechanism is unclear. In addition, the nature of the cofactor remains a controversy. Here, we report the in vitro reconstitution of the AurF enzyme activity, the crystal structure of AurF in the oxidized state, and the cocrystal structure of AurF with its product pNBA. Our combined biochemical and structural analysis unequivocally indicates that AurF is a non-heme di-iron monooxygenase that catalyzes sequential oxidation of aminoarenes to nitroarenes via hydroxylamine and nitroso intermediates.di-iron enzymes ͉ metalloenzymes ͉ N-oxygenation ͉ reaction mechanism

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“…AurF and PrnD were the first examples of N-oxygenases described, each of which are involved in the biosynthesis of aureothin and pyrrolnitrin, respectively (Choi et al, 2008;He et al, 2001;Kirner et al, 1998;Krebs et al, 2007;Lee et al, 2005;Simurdiak et al, 2006;Zhang and Parry, 2007). AurF catalyzes the formation of p-nitrobenzoate from paminobenzoate, an unusual component of the aureothin polyketide synthase.…”

Section: Us Army Engineermentioning

confidence: 99%