Thauera butanivorans sp. nov., a C2-C9 alkane-oxidizing bacterium previously referred to as 'Pseudomonas butanovora'

Dubbels, Bradley L.; Sayavedra-Soto, Luis A.; Bottomley, Peter J.; Arp, Daniel J.

doi:10.1099/ijs.0.000638-0

Cited by 54 publications

(31 citation statements)

References 17 publications

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“…This also implies the potential of a broader substrate range for the enzyme. Compared to other characterized alkane oxygenases (2,3,5,(11)(12)(13), the Pusillimonas sp. T7-7 alkane monooxygenase system shows better cold tolerance, with activity retained at temperatures as low as 0°C.…”

Section: Discussionmentioning

confidence: 99%

“…The alkylalcohol is converted to alkylaldehyde by alcohol dehydrogenase (ADH) and then to fatty acids by aldehyde dehydrogenase (ALDH) to be further degraded via the ␤-oxidation pathway. Several types of microbial alkane oxygenases have been characterized, including cytochrome P450 alkane monooxygenases, represented by the eukaryotic P450 enzyme that acts on C 10 to C 16 alkanes in Candida maltose (2) and the bacterial P450 oxygenase system that acts on C 4 to C 16 alkanes in Acinetobacter (5); the integral membrane non-heme iron alkane monooxygenases, such as AlkB in Pseudomonas that acts on C 12 to C 28 alkanes (3); and the soluble single-component monooxygenase LadA from Geobacillus thermodenitrificans NG80-2, which belongs to the bacterial luciferase SsuD subfamily and acts on long-chain alkanes (C 15 to C 36 ) (11,12). A homodimer dioxygenase with activity on C 10 to C 30 alkanes has also been found in Acinetobacter sp.…”

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confidence: 99%

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Characterization of a Novel Rieske-Type Alkane Monooxygenase System in Pusillimonas sp. Strain T7-7

Wang

Feng

2013

J Bacteriol

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The cold-tolerant bacterium Pusillimonas sp. strain T7-7 is able to utilize diesel oils (C 5 to C 30 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 (C 5 ) to tetracosane (C 24 ) using NADH as a cofactor, with greatest activity on the C 15 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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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Characterization of a Novel Rieske-Type Alkane Monooxygenase System in Pusillimonas sp. Strain T7-7

Wang

Feng

2013

J Bacteriol

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“…This genus currently consists of nine named species and one recently announced novel species (2). Organisms within Thauera have been isolated from wastewater treatment plants, where they may be a dominant part of the microbial community (3–8). They are also found in other environments, such as soils and sediments (9, 10), and are known for their versatile metabolism.…”

Section: Genome Announcementmentioning

confidence: 99%

Draft Genome Sequences of Five Strains in the Genus Thauera

2013

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“…To initiate growth on C 2 -C 9 alkanes, the Gramnegative b-proteobacterium Thauera butanivorans, formerly called 'Pseudomonas butanovora' (Dubbels et al, 2009), expresses a carboxylate-bridged non-haem di-iron monooxygenase, commonly referred to as soluble butane monooxygenase (sBMO) (Sluis et al, 2002;Takahashi et al, 1980). sBMO belongs to a family of bacterial multicomponent monooxygenases which includes soluble methane monooxygenases (sMMOs), phenol hydroxylases (PHs) and aromatic/alkene monooxygenases (TMOs) (Leahy et al, 2003;Sluis et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Kinetic characterization of the soluble butane monooxygenase from Thauera butanivorans, formerly ‘Pseudomonas butanovora’

et al. 2009

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Soluble butane monooxygenase (sBMO), a three-component di-iron monooxygenase complex expressed by the C 2 -C 9 alkane-utilizing bacterium Thauera butanivorans, was kinetically characterized by measuring substrate specificities for C 1 -C 5 alkanes and product inhibition profiles. sBMO has high sequence homology with soluble methane monooxygenase (sMMO) and shares a similar substrate range, including gaseous and liquid alkanes, aromatics, alkenes and halogenated xenobiotics. Results indicated that butane was the preferred substrate (defined by k cat : K m ratios). Relative rates of oxidation for C 1 -C 5 alkanes differed minimally, implying that substrate specificity is heavily influenced by differences in substrate K m values. The low micromolar K m for linear C 2 -C 5 alkanes and the millimolar K m for methane demonstrate that sBMO is two to three orders of magnitude more specific for physiologically relevant substrates of T. butanivorans. Methanol, the product of methane oxidation and also a substrate itself, was found to have similar K m and k cat values to those of methane. This inability to kinetically discriminate between the C 1 alkane and C 1 alcohol is observed as a steady-state concentration of methanol during the two-step oxidation of methane to formaldehyde by sBMO. Unlike methanol, alcohols with chain length C 2 -C 5 do not compete effectively with their respective alkane substrates. Results from product inhibition experiments suggest that the geometry of the active site is optimized for linear molecules four to five carbons in length and is influenced by the regulatory protein component B (butane monooxygenase regulatory component; BMOB). The data suggest that alkane oxidation by sBMO is highly specialized for the turnover of C 3 -C 5 alkanes and the release of their respective alcohol products. Additionally, sBMO is particularly efficient at preventing methane oxidation during growth on linear alkanes ¢C 2, despite its high sequence homology with sMMO. These results represent, to the best of our knowledge, the first kinetic in vitro characterization of the closest known homologue of sMMO.

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Thauera butanivorans sp. nov., a C2-C9 alkane-oxidizing bacterium previously referred to as 'Pseudomonas butanovora'

Cited by 54 publications

References 17 publications

Characterization of a Novel Rieske-Type Alkane Monooxygenase System in Pusillimonas sp. Strain T7-7

Characterization of a Novel Rieske-Type Alkane Monooxygenase System in Pusillimonas sp. Strain T7-7

Draft Genome Sequences of Five Strains in the Genus Thauera

Kinetic characterization of the soluble butane monooxygenase from Thauera butanivorans, formerly ‘Pseudomonas butanovora’

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