Characterization of the N-oxygenase AurF from Streptomyces thioletus

Chanco, Emmanuel; Choi, Yanghee; Sun, Ning; Vu, Michael; Zhao, Huimin

doi:10.1016/j.bmc.2014.06.002

Cited by 31 publications

(33 citation statements)

References 33 publications

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“…This enzyme, involved in the biosynthesis of aureothin (an antibiotic), has recently been characterized as a diiron enzyme [111], and a crystal structure has been obtained by X-ray diffraction analysis [112]. Similarly as in the catalytic cycle of CmII, an unusual μ-η 1 :η 2 -peroxo-Fe III Fe III intermediate is suggested to be the active species for the arylamine oxidation [13].…”

Section: Arylamine Oxygenases CMLI and Aurfmentioning

confidence: 99%

A growing family of O2 activating dinuclear iron enzymes with key catalytic diiron(III)-peroxo intermediates: Biological systems and chemical models

Trehoux

Mahy

Avenier

2016

Coordination Chemistry Reviews

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Section: Arylamine Oxygenases CMLI and Aurfmentioning

confidence: 99%

A growing family of O2 activating dinuclear iron enzymes with key catalytic diiron(III)-peroxo intermediates: Biological systems and chemical models

Trehoux

Mahy

Avenier

2016

Coordination Chemistry Reviews

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“…Among them, particularly relevant are the following: Ferritin111,112 and bacterioferritin, which use iron as a substrate for ferroxidation and iron storage,113 the growing subclass of bacterial multicomponent monooxygenases (BMMs;114,115 also referred to as soluble diiron monooxygenases, SDIMOs),116 including soluble methane monooxygenase (MMO), toluene/ o ‐xylene monooxygenases (ToMO), phenol hydroxylase (PH), and alkene monooxygenase (AMO), which hydroxylate a variety of organic substrates; hemerythrin (Hr) and myohemerythrin, which reversibly bind and transport oxygen;117 the ribonucleotide reductase R2 subunit (RNR‐R2), which generates a tyrosyl radical essential for the reduction of ribonucleotides to deoxyribonucleotides in DNA biosynthesis;108,118–120 the stearoyl‐acyl carrier protein (ACP) Δ 9 ‐desaturase, which introduces a double bond into saturated fatty acids 121,122. More recently, the diiron carboxylate protein family was broadened to include p ‐aminobenzoate N ‐oxygenase (AurF), which is involved in the biosynthesis of antibiotic aureothin, catalyzing the formation of p ‐nitrobenzoic acid from p ‐aminobenzoic acid,123–125 and four membrane‐associated enzymes, first identified only on the basis of six conserved amino acids, four carboxylate residues, and two histidines, which constitute the iron‐binding motif. These proteins are alternative oxidase (AOX), plastid terminal oxidase (PTOX), 5‐demethoxyquinone hydroxylase (DMQ hydroxylase), and Mg protoporphyrin IX monomethyl ester hydroxylase (MME hydroxylase) 126.…”

Section: Nature‐inspired De Novo Designmentioning

confidence: 99%

Artificial Diiron Enzymes with a De Novo Designed Four‐Helix Bundle Structure

et al. 2015

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A single polypeptide chain may provide an astronomical number of conformers. Nature selected only a trivial number of them through evolution, composing an alphabet of scaffolds, that can afford the complete set of chemical reactions needed to support life. These structural templates are so stable that they allow several mutations without disruption of the global folding, even having the ability to bind several exogenous cofactors. With this perspective, metal cofactors play a crucial role in the regulation and catalysis of several processes. Nature is able to modulate the chemistry of metals, adopting only a few ligands and slightly different geometries. Several scaffolds and metal-binding motifs are representing the focus of intense interest in the literature. This review discusses the widespread four-helix bundle fold, adopted as a scaffold for metal binding sites in the context of de novo protein design to obtain basic biochemical components for biosensing or catalysis. In particular, we describe the rational refinement of structure/function in diiron–oxo protein models from the due ferri (DF) family. The DF proteins were developed by us through an iterative process of design and rigorous characterization, which has allowed a shift from structural to functional models. The examples reported herein demonstrate the importance of the synergic application of de novo design methods as well as spectroscopic and structural characterization to optimize the catalytic performance of artificial enzymes.

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“…One is the oxidation reaction of an amino group found in chloramphenicol, aureothin, and pyrrolnitrin biosynthesis. In the former two cases, the p-amino groups of p-aminophenylalanine and p-aminobenzoic acid are oxidized to p-nitro groups using molecular oxygen as a substrate by the non-heme di-iron-containing monooxygenases CmlI (3,4) and AurF (5)(6)(7), respectively. In pyrrolnitrin biosynthesis, PrnD, which contains a Rieske iron-sulfur cluster, catalyzes the oxidation of aminopyrrolnitrin to complete the biosynthetic pathway (8).…”

mentioning

confidence: 99%

Identification and characterization of a bacterial cytochrome P450 monooxygenase catalyzing the 3-nitration of tyrosine in rufomycin biosynthesis

Tomita

Katsuyama

Minami

et al. 2017

Journal of Biological Chemistry

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Rufomycin is a circular heptapeptide with anti-mycobacterial activity and is produced by ATCC 14046. Its structure contains three non-proteinogenic amino acids,-dimethylallyltryptophan, -2-crotylglycine, and 3-nitrotyrosine (3NTyr). Although the rufomycin structure was already reported in the 1960s, its biosynthesis, including 3NTyr generation, remains unclear. To elucidate the rufomycin biosynthetic pathway, we assembled a draft genome sequence of and identified the rufomycin biosynthetic gene cluster ( cluster), consisting of 20 ORFs (). We found a putative heptamodular nonribosomal peptide synthetase encoded by , a putative tryptophan-dimethylallyltransferase encoded by , and a putative trimodular type I polyketide synthase encoded by Moreover, the cluster contains an apparent operon harboring putative cytochrome P450 () and nitric oxide synthase () genes. A similar operon, , is responsible for the formation of 4-nitrotryptophan in thaxtomin biosynthesis; the cytochrome P450 TxtE catalyzes the 4-nitration of Trp. Therefore, we hypothesized that RufO should catalyze the Tyr 3-nitration. Disruption of abolished rufomycin production by , which was restored when 3NTyr was added to the culture medium of the disruptant. Recombinant RufO protein exhibited Tyr 3-nitration activity both and Spectroscopic analysis further revealed that RufO recognizes Tyr as the substrate with a dissociation constant of ∼0.1 μm These results indicate that RufO is an unprecedented cytochrome P450 that catalyzes Tyr nitration. Taken together with the results of an analysis of the cluster, we propose a rufomycin biosynthetic pathway in.

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Characterization of the N-oxygenase AurF from Streptomyces thioletus

Cited by 31 publications

References 33 publications

A growing family of O2 activating dinuclear iron enzymes with key catalytic diiron(III)-peroxo intermediates: Biological systems and chemical models

A growing family of O2 activating dinuclear iron enzymes with key catalytic diiron(III)-peroxo intermediates: Biological systems and chemical models

Artificial Diiron Enzymes with a De Novo Designed Four‐Helix Bundle Structure

Identification and characterization of a bacterial cytochrome P450 monooxygenase catalyzing the 3-nitration of tyrosine in rufomycin biosynthesis

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