Regioelectronic factors in metabolic hydroxylation of aliphatic carbon atoms

EHT calculations have been performed on model molecules acting as substrates for mammalian mono-oxygenases. C αH bonds are consistently found to have larger overlap populations compared with C βH and C γH bonds. It is known on the other hand that metabolic hydroxylation of aliphatic carbon atoms...

Full description

Saved in:
Bibliographic Details
Published inJournal of theoretical biology Vol. 70; no. 4; pp. 339 - 344
Main Authors Testa, Bernard, Bünzli, Jean-Claude, Purcell, William P.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 20.02.1978
Subjects
Cytochrome P-450 Enzyme System - metabolism
Hydrocarbons - metabolism
Hydroxylation
Models, Biological
Oxygenases - metabolism
Online AccessGet full text

Cover

More Information
Summary:EHT calculations have been performed on model molecules acting as substrates for mammalian mono-oxygenases. C αH bonds are consistently found to have larger overlap populations compared with C βH and C γH bonds. It is known on the other hand that metabolic hydroxylation of aliphatic carbon atoms shows a marked regioselectivity for α-carbons. The quantum-mechanical results sustain the view that CH bonds of relatively high electronic density are preferred target sites for the cytochrome P-450-mediated oxygenation, and that the oxygen atom being activated is transformed into an electrophilic species capable of CH bond insertion.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0022-5193
1095-8541
DOI:10.1016/0022-5193(78)90247-3