Advances in studying bioinorganic reaction mechanisms: isotopic probes of activated oxygen intermediates in metalloenzymes.
Metalloenzymes catalyze reactions of molecular oxygen and its reduced forms through the controlled formation of metal-bound, activated oxygen intermediates. These intermediates have been a challenge to characterize and new experimental approaches capable of relating structure to reactivity under physiologically relevant conditions are needed. The application of a competitive isotope fractionation technique has enabled changes in O-O bonding to be probed during enzyme-catalyzed reactions. The derived isotope effects provide insights into the reaction mechanisms of O2 and O2*-, which probably could not have been obtained using more conventional methods.
Roth
Justine P
JP
Department of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore MD 21218, USA. jproth@jhu.edu
D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry; D055598:Chemical Phenomena; D015393:Chemistry, Bioinorganic; D004299:Dopamine beta-Hydroxylase / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D005949:Glucose Oxidase / Q000737:chemistry; D007700:Kinetics; D008670:Metals / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D010103:Oxygen Isotopes
D004798:Enzymes; D008670:Metals; D010103:Oxygen Isotopes; D005949:Glucose Oxidase; D004299:Dopamine beta-Hydroxylase; D006631:Amine Oxidase (Copper-Containing); D010100:Oxygen