Kinetics and mechanism of reductive dioxygen activation catalyzed by P-450 model system. Iron picket fence as a catalytic center
- 1 July 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 107 (15) , 4466-4473
- https://doi.org/10.1021/ja00301a016
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Study of (tetraphenylporphinato)manganese(III)-catalyzed epoxidation and demethylation using p-cyano-N,N-dimethylaniline N-oxide as oxygen donor in a homogeneous system. Kinetics, radiochemical ligation studies, and reaction mechanism for a model of cytochrome P-450Journal of the American Chemical Society, 1984
- Oxidation of monosubstituted olefins by cytochromes P-450 and heme models: Evidence for the formation of aldehydes in addition to epoxides and allylic alcoholsBiochemical and Biophysical Research Communications, 1984
- Aliphatic hydroxylation catalyzed by iron porphyrin complexesJournal of the American Chemical Society, 1983
- Epoxidation reactions catalyzed by iron porphyrins. Oxygen transfer from iodosylbenzeneJournal of the American Chemical Society, 1983
- Effective hydrogen generation system by use of ascorbic acid as a reversible electron donorThe Journal of Organic Chemistry, 1981
- Axial ligation constants of iron(II) and cobalt(II) "capped" porphyrinsJournal of the American Chemical Society, 1980
- Chemical mechanisms for cytochrome P-450 hydroxylation: evidence for acylation of heme-bound dioxygen.Proceedings of the National Academy of Sciences, 1980
- Model compounds for the T state of hemoglobin.Proceedings of the National Academy of Sciences, 1978