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Curr Opin Chem Biol. 2007 Apr;11(2):142-50. Epub 2007 Feb 16.

Advances in studying bioinorganic reaction mechanisms: isotopic probes of activated oxygen intermediates in metalloenzymes.

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1
Department of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore MD 21218, USA. jproth@jhu.edu

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.

PMID:
17307017
DOI:
10.1016/j.cbpa.2007.01.683
[Indexed for MEDLINE]
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