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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.

SUBMITTER: Paul B

PROVIDER: S-EPMC3651851 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Probing the mechanism of cyanobacterial aldehyde decarbonylase using a cyclopropyl aldehyde.

Paul Bishwajit B Das Debasis D Ellington Benjamin B Marsh E Neil G EN

Journal of the American Chemical Society 20130402 14

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 ...[more]

PMID: 23514600

Similar Datasets

Oxygen-independent decarbonylation of aldehydes by cyanobacterial aldehyde decarbonylase: a new reaction of diiron enzymes.

Project description: Not available

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| S-EPMC5132143 | biostudies-literature

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