Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1257715 | Current Opinion in Chemical Biology | 2007 | 9 Pages |
Abstract
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.
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Physical Sciences and Engineering
Chemistry
Chemistry (General)
Authors
Justine P Roth,