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Attenuation of <i>Staphylococcus aureus</i> Biofilms and Virulence by 3-Fluorocatechol. [PDF]

Antibiotics (Basel)
Kim T, Tabassum N, Javaid A, Khan F.
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Expanding clones, expanding aneurysms through macrophage-to-osteoclast differentiation. [PDF]

J Clin Invest
Regan JA, Shah SH.
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Human Tryptophan Dioxygenase:  A Comparison to Indoleamine 2,3-Dioxygenase

Journal of the American Chemical Society, 2007
In contrast to the diverse superfamily of monooxygenases, there are only two classes of heme-containing dioxygenases in humans. One is tryptophan 2,3 dioxygenase (hTDO), and the other is indoleamine 2,3-dioxygenase (hIDO), both of which catalyze the oxidative degradation of Trp to N-formyl kynurenine.
Dipanwita, Batabyal, Syun-Ru, Yeh
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NO binding to naphthalene dioxygenase

JBIC Journal of Biological Inorganic Chemistry, 2005
Nitric oxide (NO) is commonly used as an analogue for dioxygen in structural and spectroscopic studies of oxygen binding and oxygen activation. In this study, crystallographic structures of naphthalene dioxygenase (NDO) in complex with nitric oxide are reported.
Andreas, Karlsson, Juan V, Parales, Rebecca E, Parales, David T, Gibson, Hans, Eklund, S, Ramaswamy   +5 more
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Catechol dioxygenases

Essays in Biochemistry, 1999
Catechol dioxygenases are key enzymes in the metabolism of aromatic rings by soil bacteria. Catechol dioxygenases have been found that participate in the metabolism of halogenated aromatic compounds and, in doing so, play a key role in bioremediation of halogenated pollutants.
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Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase

Applied Microbiology and Biotechnology, 1999
Naphthalene 1,2-dioxygenase (Nap dox) and biphenyl 2,3-dioxygenase (Bph dox) are related enzymes that have differentiated during evolution as their specificity has changed. Although their component arrangement is similar, the structure of each component has been modified quite extensively.
D, Barriault, M, Sylvestre
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4-Hydroxyphenylpyruvate dioxygenase

Archives of Biochemistry and Biophysics, 2005
4-Hydroxyphenylpyruvate dioxygenase (HPPD) is an Fe(II)-dependent, non-heme oxygenase that catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisate. This reaction involves decarboxylation, substituent migration and aromatic oxygenation in a single catalytic cycle.
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Cysteine dioxygenase: structure and mechanism

Chemical Communications, 2007
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Joseph, CA, Maroney, MJ
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