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John T. Groves Princeton University NSF9810248 Norcarane Reveals A Radical Mechanism for Cyt P450. - PowerPoint PPT Presentation
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John T. Groves John T. Groves Princeton UniversityPrinceton University
NSF9810248NSF9810248Norcarane Reveals A Radical Mechanism for Cyt P450Norcarane Reveals A Radical Mechanism for Cyt P450
J. Am. Chem. Soc. 2002, 124, 6020-6027
P450
O2
OH OH
OH
krearr
krebound
Cytochrome P450 is the only heme protein in nature with the ability to hydroxylate simple alkanes. In collaboration with Professor Paul R. Ortiz de Montellano and postdoctoral research associate Karine Auclaire at UCSF, Princeton researchers Professor John Groves, postdoctoral research associate Zhengbo Hu and research staff member Dorothy Little have provided new insights into the mechanism of these hydrocarbon oxidation processes. With the diagnostic molecular probe norcarane, products indicative of a radical intermediate with a lifetime ranging from 16 ps to 52 ps were detected during the oxidation of norcarane by P450cam (CYP101), P450BM3 (CYP102), CYP2B1, and CYP2E1. The results provide clear support for the involvement of a two-state, radical rebound mechanism. The study, which is one of the core projects of the NSF Environmental Molecular Science Institute CEBIC, has provided new information into the ways bacteria degrade hydrocarbons in the environment.