A New Class of Arylamine Oxygenases: Evidence that p‐Aminobenzoate N‐Oxygenase (AurF) is a Di‐iron Enzyme and Further Mechanistic Studies

No abstract is available for this paper.

• Publication year

  2006

• Venue

  ChemBioChem

• Publication date

  2006-08-04

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1002/cbic.200600136PMID 16927313
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Mechanistic studies on the conversion of arylamines into arylnitro compounds by aminopyrrolnitrin oxygenase: identification of intermediates and kinetic studies.

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• Mechanistic Studies on the Conversion of Arylamines into Arylnitro Compounds by Aminopyrrolnitrin Oxygenase: Identification of Intermediates and Kinetic Studies†

  2005cited by this paper
• Sequential enzymatic oxidation of aminoarenes to nitroarenes via hydroxylamines.

  2005cited by this paper
• Reconstitution and Characterization of Aminopyrrolnitrin Oxygenase, a Rieske N-Oxygenase That Catalyzes Unusual Arylamine Oxidation*

  2005cited by this paper
• Dinuclear and mononuclear manganese(IV)-radical complexes and their catalytic catecholase activity.

  2004cited by this paper
• Biosynthetic origin of the rare nitroaryl moiety of the polyketide antibiotic aureothin: involvement of an unprecedented N-oxygenase.

  2004cited by this paper
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  2004cited by this paper
• Mechanistic implications for the formation of the diiron cluster in ribonucleotide reductase provided by quantitative EPR spectroscopy.

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• Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster.

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• Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins.

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  2018cites this paper
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