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O‐Insertion into Nonactivated CH Bonds: The first observation of O 2 cleavage by a P‐450 enzyme model in the presence of a thiolate ligand
Author(s) -
Patzelt Heiko,
Woggon WolfDietrich
Publication year - 1992
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19920750212
Subject(s) - chemistry , bond cleavage , homolysis , cleavage (geology) , stereochemistry , covalent bond , ligand (biochemistry) , insertion reaction , substrate (aquarium) , radical , catalysis , receptor , biochemistry , organic chemistry , oceanography , geotechnical engineering , fracture (geology) , geology , engineering
On reaction with ‘O’‐donors or O 2 , the synthetic P‐450 analogue 2 undergoes O‐insertion at a nonactivated CH bond of the covalently bound substrate. The mechanism of O‐insertion with O 2 most likely involves homolytic cleavage of the OO bond followed by O‐insertion via radical recombination.

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