• Publications
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4-Hydroxyphenylpyruvate dioxygenase.
  • G. Moran
  • Biology, Chemistry
    Archives of biochemistry and biophysics
  • 2005
Burkholderia cenocepacia C5424 Produces a Pigment with Antioxidant Properties Using a Homogentisate Intermediate
It is demonstrated that the brown pigment produced by B. cenocepacia C5424 is a pyomelanin synthesized from an HGA intermediate that is capable of protecting the organism from in vitro and in vivo sources of oxidative stress.
Structure of the ferrous form of (4-hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis in complex with the therapeutic herbicide, NTBC.
The three-dimensional structure of the Fe(II) form of HPPD from Streptomyces avermitilis in complex with the inhibitor 2-nitro-4-(triflouromethyl)benzoyl]-1,3-cyclohexanedione (NTBC) has been determined and is suggestive of a binding mode for the substrate and/or a transition state, which may be the origin of the exceedingly high affinity these inhibitors have for HPPD.
Two roads diverged: the structure of hydroxymandelate synthase from Amycolatopsis orientalis in complex with 4-hydroxymandelate.
The crystal structure of the hydroxymandelate synthase (HMS) reveals an overall fold that consists of two similar beta-barrel domains that contains the characteristic His/His/acid metal-coordination motif (facial triad) found in the majority of Fe2-dependent oxygenases.
The rate-limiting catalytic steps of hydroxymandelate synthase from Amycolatopsis orientalis.
Pre-steady-state analysis indicates that evidence exists for the accumulation of three intermediates in a single turnover and the decay of the third is rate-limiting in multiple turnovers.
(4-Hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis: the basis for ordered substrate addition.
The binding of ligands to HPPD from Streptomyces avermitilis is examined and data show that HPP binds to the apoenzyme and that the apo-HPPD does not bind Fe(II) to generate active holoenzyme.
Interaction of (4-hydroxyphenyl)pyruvate dioxygenase with the specific inhibitor 2-[2-nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedione.
It is proposed that the bidentate association of NTBC with the active site metal ion precedes the Lewis acid-assisted conversion of the bound enol to the enolate to form the oxidized holoenzyme, the HPPD.Fe(II).
Kynurenine 3-monooxygenase from Pseudomonas fluorescens: substrate-like inhibitors both stimulate flavin reduction and stabilize the flavin-peroxo intermediate yet result in the production of
This work has investigated the reductive and the oxidative half-reactions of a stable form of KMO from Pseudomonas fluorescens and observed the accumulation of a peroxyflavin species that then decays to yield hydrogen peroxide without hydroxylation.