ArticleJournal of inorganic biochemistry2013
Substrate specificity and reaction mechanism of purified alkane hydroxylase from the hydrocarbonoclastic bacterium Alcanivorax borkumensis (AbAlkB).
Article in Journal of inorganic biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- Deciphering biochar-PGPR-plant synergies for sustainable soil rhizoremediation of organic pollutants.Archives of microbiology · 2026Review
- Article
- No Bridge between Us: EXAFS and Computations Confirm Two Distant Iron Ions Comprise the Active Site of Alkane Monooxygenase (AlkB).Journal of the American Chemical Society · 2025Article
- Structure and Function of Alkane Monooxygenase (AlkB).Accounts of chemical research · 2023Review
- Structure and mechanism of the alkane-oxidizing enzyme AlkB.Nature communications · 2023Article
- An alkane monooxygenase (AlkB) family in which all electron transfer partners are covalently bound to the oxygen-activating hydroxylase.Journal of inorganic biochemistry · 2022Article
- An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB).Frontiers in microbiology · 2022Review
- Investigation of the prevalence and catalytic activity of rubredoxin-fused alkane monooxygenases (AlkBs).Journal of inorganic biochemistry · 2021Article
- Diversity and Oil Degradation Potential of Culturable Microbes Isolated from Chronically Contaminated Soils in Trinidad.Microorganisms · 2021Article
- Identity and mechanisms of alkane-oxidizing metalloenzymes from deep-sea hydrothermal vents.Frontiers in microbiology · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
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 CH 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.
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