title: Probing the mechanism of cyanobacterial aldehyde decarbonylase using a cyclopropyl aldehyde.
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.
authors.affiliation: Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
authors.forename: Bishwajit
authors.initials: B
authors.lastname: Paul
authors.forename: Debasis
authors.initials: D
authors.lastname: Das
authors.forename: Benjamin
authors.initials: B
authors.lastname: Ellington
authors.forename: E Neil G
authors.initials: EN
authors.lastname: Marsh
mesh_terms: D000446:Aldehyde-Lyases / Q000737:chemistry / Q000378:metabolism*; D000447:Aldehydes / Q000737:chemistry / Q000378:metabolism*; D000473:Alkanes / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D000458:Cyanobacteria / Q000201:enzymology*; D005561:Formates / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure
chemical_list: D000447:Aldehydes; D000473:Alkanes; D005561:Formates; D000446:Aldehyde-Lyases; C043439:aldehyde decarbonylase