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PubMed2001

Cross-epithelial hydrogen transfer from the midgut compartment drives methanogenesis in the hindgut of cockroaches.

In the intestinal tracts of animals, methanogenesis from CO(2) and other C(1) compounds strictly depends on the supply of electron donors by fermenting bacteria, but sources and sinks of reducing equivalents may be spatially separated. Microsensor measurements in the intestinal tract of the omnivorous cockroach Blaberus sp. showed that molecular hydrogen strongly accumulated in the midgut (H(2) partial pressures of 3 to 26 kPa), whereas it was not detectable (<0.1 kPa) in the posterior hindgut. Moreover, living cockroaches emitted large quantities of CH(4) [105 +/- 49 nmol (g of cockroach)(-1) h(-1)] but only traces of H(2). In vitro incubation of isolated gut compartments, however, revealed that the midguts produced considerable amounts of H(2), whereas hindguts emitted only CH(4) [106 +/- 58 and 71 +/- 50 nmol (g of cockroach)(-1) h(-1), respectively]. When ligated midgut and hindgut segments were incubated in the same vials, methane emission increased by 28% over that of isolated hindguts, whereas only traces of H(2) accumulated in the headspace. Radial hydrogen profiles obtained under air enriched with H(2) (20 kPa) identified the hindgut as an efficient sink for externally supplied H(2). A cross-epithelial transfer of hydrogen from the midgut to the hindgut compartment was clearly evidenced by the steep H(2) concentration gradients which developed when ligated fragments of midgut and hindgut were placed on top of each other-a configuration that simulates the situation in vivo. These findings emphasize that it is essential to analyze the compartmentalization of the gut and the spatial organization of its microbiota in order to understand the functional interactions among different microbial populations during digestion.

Animals↗
PubMed2005

Pathways for methanogenesis and diversity of methanogenic archaea in three boreal peatland ecosystems.

The main objectives of this study were to uncover the pathways used for methanogenesis in three different boreal peatland ecosystems and to describe the methanogenic populations involved. The mesotrophic fen had the lowest proportion of CH4 produced from H2-CO2. The oligotrophic fen was the most hydrogenotrophic, followed by the ombrotrophic bog. Each site was characterized by a specific group of methanogenic sequences belonging to Methanosaeta spp. (mesotrophic fen), rice cluster-I (oligotrophic fen), and fen cluster (ombrotrophic bog).

DNA, Archaeal↗
PubMed2006

Effect of inhibition of acetoclastic methanogenesis on growth of archaeal populations in an anoxic model environment.

Methyl fluoride is frequently used to specifically inhibit acetoclastic methanogenesis, thus allowing determination of the relative contribution of acetate versus H2/CO2 to total CH4 production in natural environments. However, the effect of the inhibitor on growth of the target archaeal population has not yet been studied. Therefore, we incubated rice roots as an environmental model system under anoxic conditions in the presence and absence of CH3F, measured the activity and Gibbs free energy (DeltaG) of CH4 production, and determined the abundance of individual archaeal populations by using a combination of quantitative (real-time) PCR and analysis of terminal restriction fragment length polymorphism targeting the 16S rRNA gene. It was shown that CH3F specifically inhibited not only acetoclastic methanogenic activity but also the proliferation of Methanosarcina spp, which were the prevalent acetoclastic methanogens in our environmental model system. Therefore, inhibition experiments with CH3F seem to be a suitable method for quantifying acetoclastic CH4 production. It is furthermore shown that the growth and final population size of methanogens were consistent with energetic conditions that at least covered the maintenance requirements of the population.

Acetates↗
PubMed1983

Reversal of 2-bromoethanesulfonate inhibition of methanogenesis in Methanosarcina sp.

2-Bromoethanesulfonate (BES) inhibition of methanogenesis from methanol by resting-cell suspensions or cell extracts of Methanosarcina was reversed by coenzyme M. BES inhibition of methylcoenzyme M methylreductase activity in cell-free extracts was reversed by methylcoenzyme M but not by coenzyme M. Methanol/coenzyme M methyltransferase activity was not inhibited by 10 microM BES. Inhibition of methylreductase by BES and 3-bromopropionate was competitive with methylcoenzyme M, but inhibition by 2-bromoethanol exhibited mixed kinetics. The Ki values for the inhibitors in cell-free extracts were similar to the concentrations which inhibited intact cells. BES-resistant mutants of strain 227 were apparently permeability mutants because in vitro assays showed that mutant and parent strain methylreductases were equally sensitive to BES.

Alkanesulfonates↗
PubMed1984

Formaldehyde oxidation and methanogenesis.

Formaldehyde oxidation by cell-free extracts of Methanobacterium thermoautotrophicum was shown to drive methanogenesis from CH3-S-coenzyme M or HCHO under a nonreductive atmosphere of N2. Under N2 when HCHO was the sole source of carbon and reducing equivalents in the reaction, it underwent oxidation and reduction events (disproportionation), the sum of the reactions being 3 HCHO + H2O----CH4 + 2 HCOO - + 2H+. This reaction predicts a CH4/HCHO ratio of 1/3, which is in agreement with the experimental finding of 1/2.9. In extracts of the mesophilic methanogen Methanococcus voltae and the extreme thermophile Methanococcus jannaschii , which exhibited formate dehydrogenase activity, the CH4/HCHO ratio was 1/2. NADPH stimulated methane formation from HCHO under N2. An unidentified, oxygen-labile cofactor, the formaldehyde activation factor, present in boiled-cell extract was discovered. Methanopterin , an oxygen-stable molecule, also substituted for boiled-cell extract.

Euryarchaeota↗
PubMed1985

Inhibition of methanogenesis and carbon metabolism in Methanosarcina sp. by cyanide.

NaCN was tested for its inhibitory effects on growth of and metabolism by Methanosarcina barkeri 227. NaCN (10 microM) inhibited catabolism of acetate methyl groups to CH4 and CO2 but did not inhibit methanogenesis from methanol, CO2, methylamine, or trimethylamine. NaCN also inhibited the assimilation of methanol or CO2 (as the sole carbon source) into cell carbon and stimulated the assimilation of acetate. These results suggest that inhibition by NaCN was a result of its action as an inhibitor of in vivo CO dehydrogenase. The results also implicate CO dehydrogenase in the oxidation of acetate but not methanol methyl groups to CO2.

Acetates↗
PubMed1988

Bioenergetics of methanogenesis from acetate by Methanosarcina barkeri.

Methane formation from acetate by resting cells of Methanosarcina barkeri was accompanied by an increase in the intracellular ATP content from 0.9 to 4.0 nmol/mg of protein. Correspondingly, the proton motive force increased to a steady-state level of -120 mV. The transmembrane pH gradient however, was reversed under these conditions and amounted to +20 mV. The addition of the protonophore 3,5,3',4'-tetrachlorosalicylanilide led to a drastic decrease in the proton motive force and in the intracellular ATP content and to an inhibition of methane formation. The ATPase inhibitor N,N'-dicyclohexylcarbodiimide stopped methanogenesis, and the intracellular ATP content decreased. The proton motive force decreased also under these conditions, indicating that the proton motive force could not be generated from acetate without ATP. The overall process of methane formation from acetate was dependent on the presence of sodium ions; upon addition of acetate to cell suspensions of M. barkeri, a transmembrane Na+ gradient in the range of 4:1 (Na+ out/Na+ in) was established. Possible sites of involvement of the Na+ gradient in the conversion of acetate to methane and carbon dioxide are discussed. Na+ is not involved in the CO dehydrogenase reaction.

Acetates↗
PubMed1995

Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine.

An assay which allowed detection of proteins involved in the trimethylamine- or monomethylamine (MMA)-dependent methylation of coenzyme M (CoM) was developed. The two activities could be separated by anion-exchange chromatography. The unresolved activity responsible for MMA:CoM methyl transfer eluted from a gel permeation column in the molecular mass range of 32 kDa. The activity was purified to two monomeric proteins of 40 and 29 kDa. The preparation contained protein-bound corrinoid in a mixture of Co(II) and Co(III) states, as well as methyl-B12:CoM methyltransferase (MT2) activity. N-terminal sequence analysis demonstrated that the polypeptides were two previously identified proteins of undefined physiological function. The smaller polypeptide was the monomeric 29-kDa corrinoid protein. The larger polypeptide was the "A" isozyme of MT2. Individually purified preparations of both proteins increased the rate of MMA-dependent CoM methylation by approximately 1.7 mumol/min/mg of purified protein above background activity in the extract of methanol-grown cells. These results indicate that the 29-kDa corrinoid protein and the "A" isozyme of MT2 function in methanogenesis from MMA. A likely mechanism is that the 29-kDa corrinoid is methylated by MMA and the methyl group is then transferred by the "A" isozyme of MT2 to CoM.

Amino Acid Sequence↗
PubMed1997

Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate.

During growth on acetate, Methanosarcina barkeri expresses catabolic enzymes for other methanogenic substrates such as monomethylamine. The range of substrates used by cells grown on acetate was further explored, and it was found that cells grown on acetate also converted dimethylsulfide (DMS) and methylmercaptopropionate (MMPA) to methane. Cells or extracts of cells grown on trimethylamine or methanol did not utilize either DMS or MMPA. During growth on acetate, cultures demethylated MMPA, producing methane and mercaptopropionate. Extracts of acetate-grown cells possessed DMS- and MMPA-dependent coenzyme M (CoM) methylation activities. The activity peaks of CoM methylation with either DMS or MMPA coeluted upon gel permeation chromatography of extracts of acetate-grown cells consistent with an apparent molecular mass of 470 kDa. A 480-kDa corrinoid protein, previously demonstrated to be a CoM methylase but otherwise of unknown physiological function, was found to methylate CoM with either DMS or MMPA. MMPA was demethylated by the purified 480-kDa CoM methylase, consuming 1 mol of CoM and producing 1 mol of mercaptopropionate. DMS was demethylated by the purified protein, consuming 1 mol of CoM and producing 1 mol of methanethiol. The methylthiol:CoM methyltransferase reaction could be initiated only with the enzyme-bound corrinoid in the methylated state. CoM could demethylate, and DMS and MMPA could remethylate, the corrinoid cofactor. The monomethylamine corrinoid protein and the A isozyme of methylcobamide:CoM methyltransferase (proteins homologous to the two subunits comprising the 480-kDa CoM methylase) did not catalyze CoM methylation with methylated thiols. These results indicate that the 480-kDa corrinoid protein functions as a CoM methylase during methanogenesis from DMS or MMPA.

Acetates↗
PubMed1967

Inhibition of rumen methanogenesis by methane analogues.

Extremely low concentrations of chloroform and carbon tetrachloride and somewhat larger concentrations of methylene chloride inhibited the formation of methane by the rumen microbiota in the presence or absence of added substrate. The accumulation of hydrogen at these low concentrations indicates a selective inhibition of methanogenesis. Presumably, these inhibitors affect one or more of the reactions by which methane is formed from hydrogen and carbon dioxide.

Animals↗
PubMed1992

Role of dietary sulphate in the regulation of methanogenesis in the human large intestine.

Hydrogen produced during colonic fermentation may be excreted, or removed by H2 consuming bacteria such as methanogenic and sulphate reducing bacteria. In vitro, sulphate reducing bacteria compete with methanogenic bacteria for hydrogen when sulphate is present. In this study the hypothesis that sulphate in the diet could alter CH4 production in vivo has been tested. Six methane excreting volunteers were fed a low sulphate diet (1.6 mmol/d) for 34 days with the addition of 15 mmol sodium sulphate from days 11-20. Breath methane was measured and viable counts and metabolic activities of methanogenic bacteria and sulphate reducing bacteria determined in faeces. Whole gut transit time and daily stool weight were also measured. When sulphate was added to the diet, breath methane excretion decreased in three of the subjects while faecal sulphate reduction rates rose from 7.5 (0.5) to 20.3 (4.3) nmol SO4 reduced/h/g faeces. Sulphate reducing bacteria, which were not detected during the control diet, were found and viable counts of methanogenic bacteria fell from 10(7)-10(9)/g faeces to 10(6)/g. Methanogenic counts and breath CH4 recovered after sulphate addition was stopped. No change was found in the other three subjects. Faecal weights and transit times were not different between study periods. It is concluded that methanogenesis is regulated by dietary sulphate if sulphate reducing bacteria are present. Dietary sulphate may allow growth of sulphate reducing bacteria which inhibit the growth of methanogenic bacteria. This may explain the absence of CH4 in the breath of many people in western populations.

Adult↗
PubMed2001

Influence of Ni2+ and Co2+ on methanogenic activity and the amounts of coenzymes involved in methanogenesis.

The requirement of Ni2+ and Co2+ addition on methanogenic activity and the coenzymes involved in methanogenesis were investigated in anaerobic continuous cultivation with synthetic wastewater using acetate as the sole carbon source. Addition of Ni2+ and Co2+ to the synthetic wastewater drastically increased the maximum dilution rate of the cultivation. The concentrations of coenzymes F430 and corrinoids in the biomass increased to 0.62 micromol-Ni/g-VSS and 0.67 micromol-Co/g-VSS, respectively with the increase of the dilution rate. Methanogenic activity of the culture broth also increased with an increase of dilution rate. However, without addition of Ni2+ and Co2+, F430 and corrinoids were not detected in the biomass and methanogenic activity was only a trace level at a dilution rate of 0.025 d(-1). When the amounts of Ni2+ and Co2+ added at a dilution rate of 0.6 d(-1) were lowered in steps, the concentrations of F430 and corrinoids in the biomass and methanogenic activity decreased with decreasing amounts of Ni2+ and Co2+ added. These results suggest that Ni2+ and Co2+ were required for the methane-producing reactions via increases of coenzymes F430 and corrinoids.

Journal Article↗
PubMed2003

Genomic markers of ancient anaerobic microbial pathways: sulfate reduction, methanogenesis, and methane oxidation.

Genomic markers for anaerobic microbial processes in marine sediments-sulfate reduction, methanogenesis, and anaerobic methane oxidation-reveal the structure of sulfate-reducing, methanogenic, and methane-oxidizing microbial communities (including uncultured members); they allow inferences about the evolution of these ancient microbial pathways; and they open genomic windows into extreme microbial habitats, such as deep subsurface sediments and hydrothermal vents, that are analogs for the early Earth and for extraterrestrial microbiota.

Bacteria, Anaerobic↗
PubMed1983

Monensin effects on digestibility, methanogenesis and heat increment of a cracked corn-silage diet fed to steers.

Six 300-kg steers were each fed a 70% cracked corn plus corn silage diet at two levels of intake above maintenance with and without 3 mg monensin/kg.75 body weight (W.75). A changeover design was used. Dietary energy and nitrogen were partitioned by duplicate, 22-h indirect respiration calorimetry measurements of heat and methane production on each animal concurrent with 7-d total feces and urine collection trials. Feed and feces were analyzed for energy, N, starch and neutral detergent fiber (NDF). The partial efficiency and(or) heat increment of metabolizable energy (ME) used for gain and maintenance was partitioned by regression of energy storage vs intake. At equalized gross energy intakes (adjustments made by covariance), monensin improved (P less than .01) the apparent digestibilities of energy, from 71.8 to 74.8%; NDF, from 50.5 to 57.5%, and crude protein, from 61.6 to 65.8%. Methane production averaged 5.7% of the control gross energy (GE), but was reduced by 26% (P less than .01) by monensin additions. Metabolizable energy was increased (P less than .01) from 63.3 to 66.8% of gross energy intake by monensin, resulting in an increase (P less than .01) in retained energy (64.7 to 72.3 kcal/W.75). Heat production was increased (P less than .05) by monensin, but only in proportion to the increased ME. Daily energy retentions adjusted to equal ME intake were similar with or without monensin (69.9 vs 67.1 kcal/W.75). No significant effects of monensin on the heat increment of ME use for maintenance or gain were observed. Both NEm and NEg were improved by approximately 7% by monensin; however, the relative effect on NEm vs NEg depends on method of calculation. At equalized GE intakes, approximately one-third of the improved energy utilization was explained by the reduced methanogenesis caused by monensin and two-thirds by reduced fecal losses.

Animals↗
PubMed1986

The effect of high dietary cation concentration on methanogenesis by steers fed diets with and without ionophores.

Nine steers (300 to 350 kg body weight) were divided into three groups and received either no ionophore, monensin or lasalocid in a 70% cracked corn basal diet for the entire experiment. Within each group, a 3 X 3 Latin-square design was used to evaluate the effect of a high cation concentration added to the diets on in vivo methanogenesis. The three cation treatments consisted of NaCl or KCl addition (Na or K increased to 2.5% of diet dry matter) or no cation addition. Sodium addition decreased methane production in the monensin group 19% when compared with control (P less than .05). Sodium also tended to decrease methane in the lasalocid group (P less than .1) but had no effect on the no-ionophore group. There was no significant effect of K addition on methane production when compared to no added cation. However, K tended to increase methane in both the lasalocid and no-ionophore groups and decrease methane in the monensin group. Results of this experiment support in vitro evidence that cation levels may modulate ionophore effects on methane production.

Animals↗
PubMed2002

A comparative analysis of a balance between the rates of polymer hydrolysis and acetoclastic methanogenesis during anaerobic digestion of solid waste.

A distributed model of anaerobic digestion of solid waste was developed. Waste, volatile fatty acids (VFA), methanogenic biomass and methane concentrations were the model variables. A system of parabolic partial differential equations in the one space variable and time with slab, cylindrical or spherical symmetry of the problem was solved numerically. Diffusion of VFA inhibiting both polymer hydrolysis and acetoclastic methanogenesis was taken into account. The model showed that concentration waves of methanogenic biomass and VFA propagated over reaction space. Diffusion-based "acceleration" of methane production in the reactor was possible when intensity of VFA utilisation in the methanogenic area was sufficient for complete digestion of incoming VFA. Otherwise, methanogenic area propagation would be suppressed. Optimum conditions for the solid waste digestion can be reached at low mass transfer at the beginning and at high mass transfer when methanogenic population increases. If the initial methanogenic biomass was localised at the centre of the reactor, the total reaction time was shorter as compared to the case when the initial biomass was uniformly distributed over the reactor volume. In the last case, there was no concentration wave propagation.

Bacteria, Anaerobic↗
PubMed1986

The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide.

Formylmethanofuran: tetrahydromethanopterin formyltransferase was purified to electrophoretic homogeneity from cells of Methanobacterium thermoautotrophicum. The enzyme is a tetramer of similar or identical subunits (Mr = 41,000). The equilibrium favors transfer of the formyl group to tetrahydromethanopterin (H4MPT) at physiological pH. The product of formyl transfer by the purified enzyme was shown by a number of criteria to be 5-formyl-H4MPT, as opposed to 10-formyl-H4MPT or 5,10-methenyl-H4MPT. Reconstitution of a portion of the methanogenic C1 cycle was effected by combining purified formyltransferase, methenyl-H4MPT cyclohydrolase, formylmethanofuran, and H4MPT to give methenyl-H4MPT. Additional reconstitution experiments established that the formyltransferase is an essential enzyme for the conversion of carbon dioxide to methane. In conjunction with previously published data (Donnelly, M.I., Escalante-Semerena, J.C., Rinehart, K. L., Jr., and Wolfe, R.S. (1985) Arch. Biochem. Biophys. 242, 430-439), these data substantiate the role of 5-formyl-H4MPT as an intermediate of methanogenesis.

Carbon Dioxide↗