Dataset Information

A mammalian reductive deiodinase has broad power to dehalogenate chlorinated and brominated substrates.

ABSTRACT: Iodotyrosine deiodinase is essential for iodide homeostasis and proper thyroid function in mammals. This enzyme promotes a net reductive deiodination of 3-iodotyrosine to form iodide and tyrosine. Such a reductive dehalogenation is uncommon in aerobic organisms, and its requirement for flavin mononucleotide is even more uncommon in catalysis. Reducing equivalents are now shown to transfer directly from the flavin to the halogenated substrate without involvement of other components typically included in the standard enzymatic assay. Additionally, the deiodinase has been discovered to act as a debrominase and a dechlorinase. These new activities expand the possible roles of flavin in biological catalysis and provide a foundation for determining the mechanism of this unusual process.

SUBMITTER: McTamney PM

PROVIDER: S-EPMC2758933 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

A mammalian reductive deiodinase has broad power to dehalogenate chlorinated and brominated substrates.

McTamney Patrick M PM Rokita Steven E SE

Journal of the American Chemical Society 20091001 40

Iodotyrosine deiodinase is essential for iodide homeostasis and proper thyroid function in mammals. This enzyme promotes a net reductive deiodination of 3-iodotyrosine to form iodide and tyrosine. Such a reductive dehalogenation is uncommon in aerobic organisms, and its requirement for flavin mononucleotide is even more uncommon in catalysis. Reducing equivalents are now shown to transfer directly from the flavin to the halogenated substrate without involvement of other components typically incl ...[more]

PMID: 19777994

Similar Datasets

Project description:Thermodynamic properties, i.e., bond dissociation energies and enthalpy of formation, of chlorinated and brominated polycyclic aromatic hydrocarbons play a fundamental role in understanding their formation mechanisms and reactivity. Computational electronic structure calculations routinely used to predict thermodynamic properties of various species are limited for these compounds due to large computational cost to obtain accurate results by employing high-level wave function theory methods. In this work, a number of composite model chemistry methods (CBS-QB3, G3MP2, G3, and G4) are used to compute bond dissociation energies and enthalpies of formation of small to medium-size chlorinated and brominated polycyclic aromatic hydrocarbon compounds. The enthalpy of formation is derived via the atomization method and compared against the recommended values. Statistical analysis indicates that G4 is the best method. For comparison, three commonly used density functional theory (DFT) methods (M06-2X, ωB97X-D and B2PLYP-D3) with various basis sets including 6-311++G(d, p), cc-pVTZ, and cc-pVQZ in the prediction of bond dissociation energies and enthalpies of formation have been tested using the optimized geometries at the same M06-2X/6-311++G(d, p) level of theory. It is found that ωB97X-D/6-311++G(d, p) shows the best performance in computing the bond dissociation energies, while ωB97X-D/cc-pVTZ exhibits the best prediction in enthalpy of formation of the studied reaction systems. The structural effect on the bond dissociation energies and enthalpy of formation of chlorinated and brominated polycyclic aromatic hydrocarbons are then systematically analyzed. Based on comparisons of the various methods, reliable DFT methods are recommended for future theoretical studies on large chlorinated and brominated polycyclic aromatic hydrocarbons considering both accuracy and computational cost. This work, to the authors' knowledge, is the first to systematically benchmark theoretical methods for the accurate prediction of thermodynamic properties for chlorinated and brominated polycyclic aromatic hydrocarbons.

Dataset Information

A mammalian reductive deiodinase has broad power to dehalogenate chlorinated and brominated substrates.

Publications

A mammalian reductive deiodinase has broad power to dehalogenate chlorinated and brominated substrates.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets