MASSACHUSETTS INSTITUTE OF TECHNOLOGY
The aim of this project is to understand how bacterial multicomponent monooxygenases activate dioxygen to perform the selective oxidation of hydrocarbons through the synthesis of model compounds and by direct studies of the enzymes. The flagship member of this family of proteins is methane monooxygenase but related enzymes under investigation in this project include phenol hydroxylase toluene/o-xylene monooxygenase and alkene monooxygenase. Synthetic analogs of the hydroxylase components of these enzyme systems which contains two non-heme diiron centers where O2 activation and substrate oxidation occur are constructed to study the fundamental reactions of the dioxygen with carboxylate-bridged diiron(II) centers designed to mimic the coordination geometry outside of the protein environment. The purpose of this supplement is to purchase critically needed equipment that is essential for the success of this research. The most critical need is the purchase of a ReactIR detector replacement in order to monitor the formation and decay of oxygenated-diiron species since the O?O bond vibrations provide a diagnostic spectroscopic handle in the infrared region. Also badly needed is an incubator-shaker with a gas manifold to provide the capability to grow bacteria at reduced temperature. Its refrigeration component is important for the expression of proteins at 10-13 degrees Celsius a recently realized requirement that is not available in the laboratory. These instrument and equipment requests are essential research tools needed to fulfill the objectives of this project and to accelerate the rate of progress. This supplement addresses the goal of the Recovery Act to create and retain jobs by supporting the instrument manufacturers and their affiliates.