Publications by authors named "David A Lipscomb"
Article Synopsis
- Polycyclic aromatic hydrocarbons (PAHs), like naphthalene, pose health risks due to their potential to cause cancer and genetic mutations.
- Bacteria from the genus capable of breaking down a variety of pollutants have been studied, focusing on the naphthalene dioxygenase (NDO) enzyme from strain NCIMB12038, which was characterized using electron paramagnetic resonance (EPR) and UV-Vis spectroscopy.
- The findings suggest that NDO can effectively degrade stubborn aromatic compounds, highlighting its potential for bioremediation and synthetic applications.
Rieske nonheme iron oxygenases form a large class of aromatic ring-hydroxylating dioxygenases found in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth, making them good candidates for use in synthesis of chiral intermediates and bioremediation. Studies of the chemical stability and thermostability of these enzymes thus become important.
View Article and Find Full Text PDFCrystallization and preliminary X-ray diffraction analysis of naphthalene dioxygenase from Rhodococcus sp. strain NCIMB 12038.
Acta Crystallogr D Biol Crystallogr
December 2002
The three-component naphthalene dioxygenase (NDO) enzyme system carries out the first step in the aerobic degradation of naphthalene to (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene by Rhodococcus sp. strain NCIMB 12038. The terminal oxygenase component (naphthalene 1,2-dioxygenase) that catalyzes this reaction belongs to the aromatic ring hydroxylating dioxygenase family and has been crystallized.
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