Correlating structure with function in bacterial multicomponent monooxygenases and related diiron proteins

Article Abstract:

Bacterial multicomponent monooxygenases (BMMs) catalyze the [O.sub.2]-dependent hydroxylation of hydrocarbons at a carboxylate-bridged diiron center similar to those that occur in some dimetallic oxygen-utilizing enzymes. A study seeks to understand, from a structural perspective, aspects of the diiron chemistry that control [O.sub.2] and substrate reactivity and dictate a specific outcome.

Monoamine oxidase, Iron proteins

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Modular and dynamic functionalization of polymeric scaffolds

Article Abstract:

The concepts which utilize noncovalent interactions such as hydrogen bonding, ionic interactions, electrostatic interactions, metal coordination, and [pi]-[pi] stacking in modification of copolymer side-chains to obtain multifunctional polymeric materials, induce polymer morphology changes, and influence bulk-polymer properties, are described.

Sheet Metal Work Manufacturing, Sheet metalwork, Metal Scaffolding, Usage, Design and construction, Biopolymers, Scaffolding, Metal

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Substrate trafficking and dioxygen activation in bacterial multicomponent monooxygenases

Article Abstract:

The articles discusses about the observations of the analysis of systems of a diiron (III) oxygenated intermediate with varying Mossbauer factors from analogous species in other carboxyl-bridged proteins.

Oxidases, Oxidation-reduction reaction, Oxidation-reduction reactions, Iron compounds, Mossbauer effect, Chemical properties

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