Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 11, Issue 2, Pages 142-150Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.cbpa.2007.01.683
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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 O-2 and O-2(center dot-), which probably could not have been obtained using more conventional methods.
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