G. Moran

Publications83
h-index23
Citations1,734
Highly Influential Citations61
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4-Hydroxyphenylpyruvate dioxygenase.
  • G. Moran
  • Biology, Chemistry
    Archives of biochemistry and biophysics
  • 2005
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Burkholderia cenocepacia C5424 Produces a Pigment with Antioxidant Properties Using a Homogentisate Intermediate
TLDR
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.
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Heterologous expression and purification of kynurenine-3-monooxygenase from Pseudomonas fluorescens strain 17400.
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Structure of the ferrous form of (4-hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis in complex with the therapeutic herbicide, NTBC.
TLDR
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.
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Two roads diverged: the structure of hydroxymandelate synthase from Amycolatopsis orientalis in complex with 4-hydroxymandelate.
TLDR
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.
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Structural and mechanistic comparisons of the metal-binding members of the vicinal oxygen chelate (VOC) superfamily.
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The rate-limiting catalytic steps of hydroxymandelate synthase from Amycolatopsis orientalis.
TLDR
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.
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(4-Hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis: the basis for ordered substrate addition.
TLDR
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.
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Interaction of (4-hydroxyphenyl)pyruvate dioxygenase with the specific inhibitor 2-[2-nitro-4-(trifluoromethyl)benzoyl]-1,3-cyclohexanedione.
TLDR
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).
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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…
TLDR
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.
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