Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
- G. Moran
- Biology, ChemistryArchives of biochemistry and biophysics
Burkholderia cenocepacia C5424 Produces a Pigment with Antioxidant Properties Using a Homogentisate Intermediate
- K. E. Keith, L. Killip, Panqing He, G. Moran, M. Valvano
- BiologyJournal of bacteriology
- 12 October 2007
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.
Heterologous expression and purification of kynurenine-3-monooxygenase from Pseudomonas fluorescens strain 17400.
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.
Structural and mechanistic comparisons of the metal-binding members of the vicinal oxygen chelate (VOC) superfamily.
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.
- Kayunta Johnson‐Winters, V. Purpero, M. Kavana, T. Nelson, G. Moran
- Biology, ChemistryBiochemistry
- 30 January 2003
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.