Phylogenetic analysis of 18 thermophilic Methanobacterium isolates supports the proposals to create a new genus, Methanothermobacter gen. nov., and to reclassify several isolates in three species, Methanothermobacter thermautotrophicus comb. nov., Methanothermobacter wolfeii comb. nov., and Methanothermobacter marburgensis sp. nov.

Wasserfallen, Alain; Nölling, J; Pfister, Peter; Reeve, John N.; Macario, Everly Conway de

doi:10.1099/00207713-50-1-43

Cited by 238 publications

(152 citation statements)

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“…Aerobically harvested frozen cells from a pure culture of Methanobacter thermautotrophicus (previously known as Methanobacterium thermoautotrophicum) [23], grown at 70°C, were refluxed in methanolic HCl (4.8 M, 4 h) to cleave phosphatidyl and glycosyl headgroups, before liberated core tetraether lipids were partitioned into dichloromethane (DCM). The organic extract was reduced in vacuo and taken to dryness by evaporation under a stream of nitrogen before isolation of tetraether lipids by flash column chromatography on an activated alumina column (approximately 7 ϫ 50 mm), drypacked in a Pasteur pipette and fully solvated with hexane/DCM (9:1 vol/vol).…”

Section: Sample Preparationmentioning

confidence: 99%

Rapid discrimination of archaeal tetraether lipid cores by liquid chromatography-tandem mass spectrometry

Knappy

Chong

Keely

2009

J. Am. Soc. Mass Spectrom.

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Atmospheric pressure chemical ionization liquid chromatography-tandem mass spectrometry (APCI LC-MS/MS) of tetraether lipid cores of archaeal origin reveals distinct dissociation pathways for three classes of core lipid extracted from Methanobacter thermautotrophicus. Within these classes, two isobaric tetraether lipids, one a scarcely reported lipid constituent of M. thermautotrophicus and the other an artefact formed during extraction from cultured cells, were identified and distinguished via their MS 2 spectra. APCI LC-MS/MS discriminates different tetraether core lipid types and isobaric species and reveals the mass of the constituent biphytanyl chains within the tetraether cores, albeit without full elucidation of their structures. Furthermore, the method allows direct estimation of the relative proportions of tetraether core lipids from chromatographic peak area measurement, allowing rapid profiling of these compounds in microbiological and environmental extracts. (J Am Soc Mass Spectrom 2009, 20, 51-59)

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Section: Sample Preparationmentioning

confidence: 99%

Rapid discrimination of archaeal tetraether lipid cores by liquid chromatography-tandem mass spectrometry

Knappy

Chong

Keely

2009

J. Am. Soc. Mass Spectrom.

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“…Four different species of methanogens were utilized in these studies: Methanothermobacter marburgensis (OCM 82, formerly referred to as Methanobacterium thermautotrophicum strain Marburg, see Wasserfallen et al 2000), supplied by D. Boone; Methanosarcina barkeri strain 227 (OCM 35), also supplied by D. Boone; Methanosaeta thermophila strain CALS-1 (DSMZ 3870), supplied by S. Zinder; and Methanosaeta concilii strain GP6 (DSMZ 3671), supplied by A. Chidthaisong. All precultures were grown in 1-l crimp-top culture bottles using the technique of Hungate (1969).…”

Section: Organisms and Growth Conditionsmentioning

confidence: 99%

Hydrogen production by methanogens under low-hydrogen conditions

Valentine

Blanton

Reeburgh

2000

Archives of Microbiology

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Hydrogen production was studied in four species of methanogens (Methanothermobacter marburgensis, Methanosaeta thermophila, Methanosarcina barkeri, and Methanosaeta concilii) under conditions of low (sub-nanomolar) ambient hydrogen concentration using a specially designed culture apparatus. Transient hydrogen production was observed and quantified for each species studied. Methane was excluded as the electron source, as was all organic material added during growth of the cultures (acetate, yeast extract, peptone). Hydrogen production showed a strong temperature dependence, and production ceased at temperatures below the growth range of the organisms. Addition of polysulfides to the cultures greatly decreased hydrogen production. The addition of bromoethanesulfonic acid had little influence on hydrogen production. These experiments demonstrate that some methanogens produce excess reducing equivalents during growth and convert them to hydrogen when the ambient hydrogen concentration becomes low. The lack of sustained hydrogen production by the cultures in the presence of methane provides evidence against "reverse methanogenesis" as the mechanism for anaerobic methane oxidation.

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“…Moreover, the purification of the enzyme from Archaea that thrive in extreme environments is complicated by the difficulty of growing these organisms in a laboratory. Two reports of purified SHMT activity, from Methanobacterium thermoautotrophicum (4), recently renamed Methanothermobacter marburgensis (5), and from Sulfolobus solfataricus (6), with limited structural and functional characterization, have been made. In the first report, the enzyme was proposed to function in vivo in the direction of serine biosynthesis.…”

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confidence: 99%

Catalytic and Thermodynamic Properties of Tetrahydromethanopterin-dependent Serine Hydroxymethyltransferase from Methanococcus jannaschii

Angelaccio¹,

Chiaraluce²,

Consalvi³

et al. 2003

Journal of Biological Chemistry

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The reaction catalyzed by serine hydroxymethyltransferase (SHMT), the transfer of C␤ of serine to tetrahydropteroylglutamate, represents in Eucarya and Eubacteria a major source of one-carbon (C 1 ) units for several essential biosynthetic processes. In many Archaea, C 1 units are carried by modified pterin-containing compounds, which, although structurally related to tetrahydropteroylglutamate, play a distinct functional role. Tetrahydromethanopterin, and a few variants of this compound, are the modified folates of methanogenic and sulfate-reducing Archaea. Little information on SHMT from Archaea is available, and the metabolic role of the enzyme in these organisms is not clear. This contribution reports on the purification and characterization of recombinant SHMT from the hyperthermophilic methanogen Methanococcus jannaschii. The enzyme was characterized with respect to its catalytic, spectroscopic, and thermodynamic properties. Tetrahydromethanopterin was found to be the preferential pteridine substrate. Tetrahydropteroylglutamate could also take part in the hydroxymethyltransferase reaction, although with a much lower efficiency. The catalytic features of the enzyme with substrate analogues and in the absence of a pteridine substrate were also very similar to those of SHMT isolated from Eucarya or Eubacteria. On the other hand, the M. jannaschii enzyme showed increased thermoactivity and resistance to denaturating agents with respect to the enzyme purified from mesophilic sources. The results reported suggest that the active site structure and the mechanism of SHMT are conserved in the enzyme from M. jannaschii, which appear to differ only in its ability to bind and use a modified folate as substrate and increased thermal stability.Serine hydroxymethyltransferase (SHMT, 1 EC 2.1.2.1) catalyzes the reversible transfer of C␤ of serine to tetrahydropteroylglutamate (H 4 PteGlu) to form glycine and 5,10-methylene-H 4 PteGlu. In Eukarya and Eubacteria, H 4 PteGlu functions as a carrier of C 1 units in several oxidation states, which are used in the biosynthesis of important cellular components, such as purines and thymidylate, in the regeneration of methionine from homocysteine or, in acetogenic bacteria, in the synthesis of acetyl-CoA. The reaction catalyzed by SHMT represents in these organisms one of the major loading routes of C 1 units onto the folate carrier (1). In methanogens and several other Archaea, C 1 fragments from formyl to methyl oxidation levels are carried by tetrahydromethanopterin (H 4 MPT), a pterin-containing compound involved in methanogenesis. Although H 4 PteGlu and H 4 MPT are structurally similar in their pterin-like portion (Fig. 1) and in the role as C 1 units carriers, they are functionally distinct. H 4 MPT does not appear to be suited to most of the biosynthetic functions of H 4 PteGlu. Moreover, the biosynthetic pathways of the two carriers have few, if any, homologies, suggesting the possibility of separate evolutionary origins (2). In the metabolism of folates, SHMT represents a...

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Cited by 238 publications

References 32 publications

Rapid discrimination of archaeal tetraether lipid cores by liquid chromatography-tandem mass spectrometry

Rapid discrimination of archaeal tetraether lipid cores by liquid chromatography-tandem mass spectrometry

Hydrogen production by methanogens under low-hydrogen conditions

Catalytic and Thermodynamic Properties of Tetrahydromethanopterin-dependent Serine Hydroxymethyltransferase from Methanococcus jannaschii

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