Probing the Mechanism of Cyanobacterial Aldehyde Decarbonylase
Using a Cyclopropyl Aldehyde
- Publication date
- Publisher
Abstract
Cyanobacterial aldehyde
decarbonylase (cAD) is a non-heme diiron
oxygenase that catalyzes the conversion of fatty aldehydes to alkanes
and formate. The mechanism of this chemically unusual reaction is
poorly understood. We have investigated the mechanism of C1–C2
bond cleavage by cAD using a fatty aldehyde that incorporates a cyclopropyl
group, which can act as a radical clock. When reacted with cAD, the
cyclopropyl aldehyde produces 1-octadecene as the rearranged product,
providing evidence for a radical mechanism for C–C bond scission.
In an alternate pathway, the cyclopropyl aldehyde acts as a mechanism-based
irreversible inhibitor of cAD through covalent binding of the alkyl
chain to the enzyme