Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1301038 | Coordination Chemistry Reviews | 2013 | 25 Pages |
•Metalloenzyme-catalyzed aliphatic carbon–carbon bond cleavage reactions recently identified.•Substrates vary in terms of their O2 reactivity in the absence of enzyme.•Reaction pathways depend on the nature of the substrate; metal versus substrate reactivity with O2.•Regioselectivity of carbon–carbon bond cleavage influenced by nature of metal ion.•Model systems providing insight into structure/reactivity relationships.
Over the past decade, several metalloenzymes have been characterized which catalyze dioxygenase-type aliphatic carbon–carbon bond cleavage reactions. The substrates for these enzymes vary from species that are stable with respect to O2 under ambient conditions, to examples that in anionic form exhibit O2 reactivity in the absence of enzyme. Described herein are advances from studies of the enzymes themselves and model systems. These combined investigations provide insight into novel mechanistic pathways leading to aliphatic carbon–carbon bond cleavage and/or the factors that influence regioselectivity in the oxidative carbon–carbon bond cleavage reactions.
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