EC Number   |
General Information |
Reference |
|---|
  1.14.99.68 | physiological function |
AurF is a non-heme di-iron monooxygenase that catalyzes sequential oxidation of aminoarenes to nitroarenes via hydroxylamine and nitroso intermediates |
760058 |
| 1.14.99.68 | physiological function |
comparison with aminopyrrolnitrin oxygenase (PrnD). Hydroxylamine and nitroso intermediates are invoved in oxygenation reaction of arylamines |
758639 |
| 1.14.99.68 | physiological function |
in-frame deletion of aurF yields a mutant, in which both N-oxidation activity and aureothin production is abolished. Aureothin biosynthesis in the mutant can be fully restored upon supplying the culture with synthetic 4-nitrobenzoate |
759393 |
| 1.14.99.68 | physiological function |
peroxo-Fe2 III-III AurF oxidizes 4-hydroxylaminobenzoate Ar-NHOH. This reaction proceeds through to the Ar-NO2 final product, a four-electron oxidation, and produces Fe2 II-II AurF, with which O2 can combine to regenerate peroxo-Fe2 III-III AurF. Conversion of Ar-NHOH to Ar-NO2 requires only a single equivalent of O2 is fully catalytic in the absence of exogenous reducing equivalents |
760059 |
| 1.14.99.68 | physiological function |
reduced AurF's electronic and geometric structures are poised to react rapidly with O2. The active peroxo intermediate has a protonated peroxo bridge. The protonation activates peroxide for electrophilic/single-electron-transfer reactivity |
759403 |
| 1.14.99.68 | physiological function |
the Fe2 II/II cluster in AurF reacts with O2 in the absence of substrate to form a stable (half-life of about 7 min at 20°C) adduct with spectroscopic properties characteristic of a peroxo-Fe2 III/III complex. The intermediate complex decays rapidly (half-life of about 0.005 s at 20°C) when mixed with stoichiometric 4-aminobenzoate. Over 80% conversion of 4-aminobenzoate to 4-nitrobenzoate is observed upon addition of less than 0.3 equivalents of the amine substrate to a solution of the intermediate peroxo-Fe2 III/III complex. The complex might effect all three steps in the sequence |
759394 |
| 1.14.99.68 | physiological function |
the key oxygenated intermediates in diiron arylamine oxygenases AurF and CmlI, EC 1.14.99.67, so-called P, are uniformly hydroperoxo species having similar structures rather than the believed peroxo species. A diferric-hydroperoxo P is proposed to be able to promote the arylamine N-oxygenation with highly accessible kinetics |
759400 |
