A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus

Victoria Korneeva Korboukh, Ning Li, Eric W. Barr, Joseph M. Bollinger, Jr., Carsten Krebs

Research output: Contribution to journalArticle

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Abstract

(Chemical Equation Presented) The amine oxygenase AurF from Streptomyces thioluteus catalyzes the six-electron oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA). In this work, we have studied the reaction of its reduced Fe2(II/II) cofactor with O2, which results in generation of a peroxo-Fe2(III/III) intermediate. In the absence of substrate, this intermediate is unusually stable (t1/2 = 7 min at 20°C), allowing for its accumulation to almost stoichiometric amounts. Its decay is accelerated 105-fold by the substrate, pABA, implying that it is the complex that effects the two-electron oxidation of the amine to the hydroxylamine. The nearly quantitative conversion of pABA to pNBA by solutions containing an excess of the intermediate suggests that it may also be competent for the two subsequent two-electron oxidations leading to the product.

Original languageEnglish (US)
Pages (from-to)13608-13609
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number38
DOIs
StatePublished - Oct 13 2009

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para-Aminobenzoates
Oxygenases
Streptomyces
Nitrobenzoates
Amines
Electrons
Oxidation
Substrates
Hydroxylamine

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

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title = "A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus",
abstract = "(Chemical Equation Presented) The amine oxygenase AurF from Streptomyces thioluteus catalyzes the six-electron oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA). In this work, we have studied the reaction of its reduced Fe2(II/II) cofactor with O2, which results in generation of a peroxo-Fe2(III/III) intermediate. In the absence of substrate, this intermediate is unusually stable (t1/2 = 7 min at 20°C), allowing for its accumulation to almost stoichiometric amounts. Its decay is accelerated 105-fold by the substrate, pABA, implying that it is the complex that effects the two-electron oxidation of the amine to the hydroxylamine. The nearly quantitative conversion of pABA to pNBA by solutions containing an excess of the intermediate suggests that it may also be competent for the two subsequent two-electron oxidations leading to the product.",
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year = "2009",
month = "10",
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A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus. / Korboukh, Victoria Korneeva; Li, Ning; Barr, Eric W.; Bollinger, Jr., Joseph M.; Krebs, Carsten.

In: Journal of the American Chemical Society, Vol. 131, No. 38, 13.10.2009, p. 13608-13609.

Research output: Contribution to journalArticle

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N2 - (Chemical Equation Presented) The amine oxygenase AurF from Streptomyces thioluteus catalyzes the six-electron oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA). In this work, we have studied the reaction of its reduced Fe2(II/II) cofactor with O2, which results in generation of a peroxo-Fe2(III/III) intermediate. In the absence of substrate, this intermediate is unusually stable (t1/2 = 7 min at 20°C), allowing for its accumulation to almost stoichiometric amounts. Its decay is accelerated 105-fold by the substrate, pABA, implying that it is the complex that effects the two-electron oxidation of the amine to the hydroxylamine. The nearly quantitative conversion of pABA to pNBA by solutions containing an excess of the intermediate suggests that it may also be competent for the two subsequent two-electron oxidations leading to the product.

AB - (Chemical Equation Presented) The amine oxygenase AurF from Streptomyces thioluteus catalyzes the six-electron oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA). In this work, we have studied the reaction of its reduced Fe2(II/II) cofactor with O2, which results in generation of a peroxo-Fe2(III/III) intermediate. In the absence of substrate, this intermediate is unusually stable (t1/2 = 7 min at 20°C), allowing for its accumulation to almost stoichiometric amounts. Its decay is accelerated 105-fold by the substrate, pABA, implying that it is the complex that effects the two-electron oxidation of the amine to the hydroxylamine. The nearly quantitative conversion of pABA to pNBA by solutions containing an excess of the intermediate suggests that it may also be competent for the two subsequent two-electron oxidations leading to the product.

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