Journal
JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 121, Issue -, Pages 46-52Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2012.12.012
Keywords
Alkane hydroxylase; Alkane oxidation; Hydrocarbonoclastic; AlkB
Funding
- NIH grant [R15GM072506-02]
- National Science Foundation [CHE-0616633, CHE-1148597]
- Beckman Undergraduate Research Fellowship
- National Center for Research Resources [5P20RR016463]
- National Institute of General Medical Sciences from the National Institutes of Health [8 P20 GM103423]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1148597] Funding Source: National Science Foundation
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An alkane hydroxylase from the marine organism Alcanivorax borkumensis (AbAlkB) was purified. The purified protein retained high activity in an assay with purified rubredoxin (AlkG), purified maize ferredoxin reductase, NADPH, and selected substrates. The reaction mechanism of the purified protein was probed using the radical clock substrates bicyclo[4.1.0]heptane (norcarane), bicyclo[3.1.0]hexane (bicyclohexane), methylphenylcyclopropane and deuterated and non-deuterated cyclohexane. The distribution of products from the radical clock substrates supports the hypothesis that purified AbAlkB hydroxylates substrates by forming a substrate radical. Experiments with deuterated cyclohexane indicate that the rate-determining step has a significant C-H bond breaking character. The products formed from a number of differently shaped and sized substrates were characterized to determine the active site constraints of this AlkB. AbAlkB can catalyze the hydroxylation of a large number of aromatic compounds and linear and cyclic alkanes. It does not catalyze the hydroxylation of alkanes with a chain length longer than 15 carbons, nor does it hydroxylate sterically hindered C-H bonds. (c) 2012 Elsevier Inc. All rights reserved.
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