ArticleJournal of inorganic biochemistry2022
An alkane monooxygenase (AlkB) family in which all electron transfer partners are covalently bound to the oxygen-activating hydroxylase.
Article in Journal of inorganic biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Salinity-driven microbial adaptation of hydrocarbon-degrading communities in coastal sediments.mSphere · 2026Article
- Aerobic catabolism of isobutylene byApplied and environmental microbiology · 2026Article
- Engineering membrane-bound alkane monooxygenase from Marinobacter sp. for increased activity in the selective ω-hy-droxylation of linear and branched aliphatic esters.Protein science : a publication of the Protein Society · 2026Article
- Redirecting linear hydrocarbon metabolism toward polyhydroxyalkanoate biosynthesis.Microbial cell factories · 2026Article
- Versatile roles of rubredoxin reductase of Pseudomonas aeruginosa TBCF10839 in virulence and stress protection.PLoS pathogens · 2025Article
- Metabolic characterization of alkane monooxygenases and the growth phenotypes ofJournal of bacteriology · 2025Article
- Article
- High hydrostatic pressure stimulates n-CCommunications biology · 2025Article
- Metabolic engineering ofFrontiers in bioengineering and biotechnology · 2025Article
- Structure and Function of Alkane Monooxygenase (AlkB).Accounts of chemical research · 2023Review
- Genome-Wide Expression Analysis Unravels Fluoroalkane Metabolism inEnvironmental science & technology · 2023Article
- An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB).Frontiers in microbiology · 2022Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Alkane monooxygenase (AlkB) is a non-heme diiron enzyme that catalyzes the hydroxylation of alkanes. It is commonly found in alkanotrophic organisms that can live on alkanes as their sole source of carbon and energy. Activation of AlkB occurs via two-electron reduction of its diferric active site, which facilitates the binding, activation, and cleavage of molecular oxygen for insertion into an inert CH bond. Electrons are typically supplied by NADH via a rubredoxin reductase (AlkT) to a rubredoxin (AlkG) to AlkB, although alternative electron transfer partners have been observed. Here we report a family of AlkBs in which both electron transfer partners (a ferredoxin and a ferredoxin reductase) appear as an N-terminal gene fusion to the hydroxylase (ferr_ferrR_AlkB). This enzyme catalyzes the hydroxylation of medium chain alkanes (C6-C14), with a preference for C10-C12. It requires only NADH for activity. It is present in a number of bacteria that are known to be human pathogens. A survey of the genome neighborhoods in which is it found suggest it may be involved in alkane metabolism, perhaps facilitating growth of pathogens in non-host environments.
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