ArticleJournal of bacteriology2013
Characterization of a novel Rieske-type alkane monooxygenase system in Pusillimonas sp. strain T7-7.
Article in Journal of bacteriology, 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.
- Exploring the Potential and Evaluating Hydrocarbon Degradation by Novel Antarctic Dietzia and Pusillimonas Isolates From a Pristine Environment.Environmental microbiology reports · 2026Article
- Transcriptomic changes in barley leaves induced by alcohol ethoxylates indicate potential pathways of surfactant detoxification.Scientific reports · 2024Article
- Purification and characterization of a Rieske oxygenase and its NADH-regenerating partner proteins.Methods in enzymology · 2024Article
- Contrasting Mechanisms of Aromatic and Aryl-Methyl Substituent Hydroxylation by the Rieske Monooxygenase Salicylate 5-Hydroxylase.Biochemistry · 2023Article
- A Structural View of Alkyl-Coenzyme M Reductases, the First Step of Alkane Anaerobic Oxidation Catalyzed by Archaea.Biochemistry · 2022Review
- Mining of two novel aldehyde dehydrogenases (DHY-SC-VUT5 and DHY-G-VUT7) from metagenome of hydrocarbon contaminated soils.BMC biotechnology · 2021Article
- Potential for and Distribution of Enzymatic Biodegradation of Polystyrene by Environmental Microorganisms.Materials (Basel, Switzerland) · 2021Article
- Article
- Survival and Energy Producing Strategies of Alkane Degraders Under Extreme Conditions and Their Biotechnological Potential.Frontiers in microbiology · 2018Review
- Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases.AMB Express · 2017Article
- Diverse alkane hydroxylase genes in microorganisms and environments.Scientific reports · 2014Article
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3 authors.
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Abstract
The cold-tolerant bacterium Pusillimonas sp. strain T7-7 is able to utilize diesel oils (C5 to C30 alkanes) as a sole carbon and energy source. In the present study, bioinformatics, proteomics, and real-time reverse transcriptase PCR approaches were used to identify the alkane hydroxylation system present in this bacterium. This system is composed of a Rieske-type monooxygenase, a ferredoxin, and an NADH-dependent reductase. The function of the monooxygenase, which consists of one large (46.711 kDa) and one small (15.355 kDa) subunit, was further studied using in vitro biochemical analysis and in vivo heterologous functional complementation tests. The purified large subunit of the monooxygenase was able to oxidize alkanes ranging from pentane (C5) to tetracosane (C24) using NADH as a cofactor, with greatest activity on the C15 substrate. The large subunit also showed activity on several alkane derivatives, including nitromethane and methane sulfonic acid, but it did not act on any aromatic hydrocarbons. The optimal reaction condition of the large subunit is pH 7.5 at 30°C. Fe(2+) can enhance the activity of the enzyme evidently. This is the first time that an alkane monooxygenase system belonging to the Rieske non-heme iron oxygenase family has been identified in a bacterium.
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