Spectroscopic and Computational Studies of Mononuclear Nonheme Iron Enzymes
Author | : Kenneth M. Light |
Publisher | : |
Total Pages | : |
Release | : 2014 |
ISBN-10 | : OCLC:878503472 |
ISBN-13 | : |
Rating | : 4/5 (72 Downloads) |
Download or read book Spectroscopic and Computational Studies of Mononuclear Nonheme Iron Enzymes written by Kenneth M. Light and published by . This book was released on 2014 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Mononuclear nonheme iron enzymes (NH Fe enzymes) catalyze a variety of biological reactions. A large group of NH Fe enzymes use a ferrous active site to activate dioxygen towards reaction with substrate, and require an additional cofactor as a source of electrons necessary for catalysis. The main part of this thesis involves the application of a circular dichroism (CD), magnetic circular dichroism (MCD) and variable temperature, variable-field MCD (VTVH MCD) spectroscopic methodology to a series of alpha-ketoglurate-dependent (alpha-KG-dependent) enzymes for the purpose of understanding how this enzyme family and the NH Ferrous enzymes in general induce the dissociation the generation of a 5C site for dioxgyen reactivity, as well as how dioxygen binding is oriented for proper catalysis. In addition to catalyzing oxidation of organic substrates, NH Fe enzymes are also involved in the catalytic hydrolysis and hydration of substrates. A prominent example of this is nitrile hydratases (NHases), unusual low-spin (LS) Ferric or Cobaltic enzymes that catalyze the conversion of nitriles to amides in soil bacteria. Another part of this thesis involves the spectroscopic characterization of a ferric NHase for the determination of its active site geometric and electronic structure, which are used to calibrate a computational model which is extended to explore the NHase catalytic mechanism.