Radical Clock Substrates, Their C−H Hydroxylation Mechanism by Cytochrome P450, and Other Reactivity Patterns: What Does Theory Reveal about the Clocks' Behavior?
Author:
Affiliation:
1. Contribution from the Department of Organic Chemistry and the Lise-Meitner-Minerva Center for Computational Quantum Chemistry, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja039439s
Reference60 articles.
1. (a) Groves, Y.Z.; Han, J. T. InCytochrome P450: Structure,Mechanism and Biochemistry, 2nd ed.; Ortiz de Montellano, P. R., Ed.; Plenum Press: New York, 1995; pp 3−48.
2. The bioinorganic chemistry of iron in oxygenases and supramolecular assemblies
3. Key elements of the chemistry of cytochrome P-450: The oxygen rebound mechanism
4. Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450. Evidence for a carbon radical intermediate
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