ArticleJournal of inorganic biochemistry2021
Investigation of the prevalence and catalytic activity of rubredoxin-fused alkane monooxygenases (AlkBs).
Article in Journal of inorganic biochemistry, 2021. 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, 22 citations in OpenAlex.
- 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
- Article
- Potentiation of Catalase-Mediated Plant Thermotolerance by N-Terminal Attachment of Solubilizing/Thermostabilizing Fusion Partners.International journal of molecular sciences · 2024Article
- Structure and Function of Alkane Monooxygenase (AlkB).Accounts of chemical research · 2023Review
- Structure and mechanism of the alkane-oxidizing enzyme AlkB.Nature communications · 2023Article
- Structural basis for enzymatic terminal C-H bond functionalization of alkanes.Nature structural & molecular biology · 2023Article
- Current Advances in Biodegradation of Polyolefins.Microorganisms · 2022Review
- Periodic TableTalks: An Oasis of Science within a Conference Desert.Inorganic chemistry · 2022Article
- 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
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Interest in understanding the environmental distribution of the alkane monooxygenase (AlkB) enzyme led to the identification of over 100 distinct alkane monooxygenase (AlkB) enzymes containing a covalently bound, or fused, rubredoxin. The rubredoxin-fused AlkB from Dietzia cinnamea was cloned as a full-length protein and as a truncated protein with the rubredoxin domain deleted. A point mutation (V91W) was introduced into the full-length protein, with the goal of assessing how steric bulk in the putative substrate channel might affect selectivity. Based on activity studies with alkane and alkene substrates, the rubredoxin-fused AlkB oxidizes a similar range of alkane substrates relative to its rubredoxin domain-deletion counterpart. Oxidation of terminal alkenes generated both an epoxide and a terminal aldehyde. The products of V91W-mutant-catalyzed oxidation of alkenes had a higher aldehyde-to-epoxide ratio than the products formed in the presence of the wild type protein. These results are consistent with this mutation causing a structural change impacting substrate positioning.
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