Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1257448 | Current Opinion in Chemical Biology | 2009 | 15 Pages |
Abstract
FeIIIOOH and FeIVO intermediates have now been documented in a number of nonheme iron active sites. In this Current Opinion we use spectroscopy combined with electronic structure calculations to define the frontier molecular orbitals (FMOs) of these species and their contributions to reactivity. For the low-spin FeIIIOOH species in activated bleomycin we show that the reactivity of this nonheme iron intermediate is very different from that of the analogous Compound 0 of cytochrome P450. For FeIVO S = 1 model species we experimentally define the electronic structure and its contribution to reactivity, and computationally evaluate how this would change for the FeIVO S = 2 intermediates found in nonheme iron enzymes.
Related Topics
Physical Sciences and Engineering
Chemistry
Chemistry (General)
Authors
Edward I Solomon, Shaun D Wong, Lei V Liu, Andrea Decker, Marina S Chow,