Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 19, Issue 12, Pages 4058-4068Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201202811
Keywords
biomimetics; cytochromes; O-O activation; hydrogen; oxido ligands
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Funding
- Petroleum Technology Development Fund (PTDF) of the Nigerian Government
- US Department of Energy, Office of Basic Energy Science [DE-FG02-06ER15799]
- EPSRC [EP/J003921/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/J003921/1] Funding Source: researchfish
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Iron(IV)oxo intermediates are involved in oxidations catalyzed by heme and nonheme iron enzymes, including the cytochromes P450. At the distal site of the heme in P450 CompoundI (FeIVoxo bound to porphyrin radical), the oxo group is involved in several hydrogen-bonding interactions with the protein, but their role in catalysis is currently unknown. In this work, we investigate the effects of hydrogen bonding on the reactivity of high-valent metaloxo moiety in a nonheme iron biomimetic model complex with trigonal bipyramidal symmetry that has three hydrogen-bond donors directed toward a metal(IV)oxo group. We show these interactions lower the oxidative power of the oxidant in reactions with dehydroanthracene and cyclohexadiene dramatically as they decrease the strength of the OH bond (BDEOH) in the resulting metal(III)hydroxo complex. Furthermore, the distal hydrogen-bonding effects cause stereochemical repulsions with the approaching substrate and force a sideways attack rather than a more favorable attack from the top. The calculations, therefore, give important new insights into distal hydrogen bonding, and show that in biomimetic, and, by extension, enzymatic systems, the hydrogen bond may be important for proton-relay mechanisms involved in the formation of the metaloxo intermediates, but the enzyme pays the price for this by reduced hydrogen atom abstraction ability of the intermediate. Indeed, in nonheme iron enzymes, where no proton relay takes place, there generally is no donating hydrogen bond to the iron(IV)oxo moiety.
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