| Autor: |
John T. Groves, Thomas E. Nemo |
| Rok vydání: |
1983 |
| Předmět: |
|
| Zdroj: |
The Coordination Chemistry of Metalloenzymes ISBN: 9789400970519 |
| DOI: |
10.1007/978-94-009-7049-6_28 |
| Popis: |
Evidence has emerged over the last decade to support an intermediate heme-ironoxo complex as the active oxygen species in the catalytic cycle of cytochrome P-450. Studies with deuterated substrates have shown that a large isotope effect and significant rearrangement accompany the aliphatic hydroxylation mediated by this enzyme. Model studies with chromium, manganese and iron porphyrins have shown that the latter stages of oxygen transfer can be simulated outside of the protein. An oxochromium (V) porphyrin complex has been characterized by its e. s. r. spectrum. An X-ray crystal structure of our oxochromium(IV) complex has been determined. An oxomanganese(V) porphyrin complex has been shown to hydroxylate alkanes under mild conditions. An iron(IV) porphyrin cation radical species which has spectroscopic features similar to those reported for peroxidase Compound I has been shown to transfer oxygen to hydrocarbon substrates. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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