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Methanosarcina barkeri

About: Methanosarcina barkeri is a research topic. Over the lifetime, 703 publications have been published within this topic receiving 32151 citations.


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Journal ArticleDOI
TL;DR: The effect of bioaugmentation with different microorganisms on anaerobic digestion to mitigate the ammonia inhibition problem was investigated in this paper, where seven pure strains of microorganisms (including obligate aceticlastic methanogen, facultative acetic lastic methenogen, hydrogenotrophic methanogenesis, syntrophic acetate oxidizing bacteria (SAOB), and SAOB Syntrophaceticu schinkii together was the optimal choice, methane production (MP) was 71.1% higher than that in Blank, the activity of HOG was greatly

114 citations

Journal ArticleDOI
TL;DR: The methanol-activating MtaBC complex from Methanosarcina barkeri composed of the zinc-containing MtaB and the 5-hydroxybenzimidazolylcobamide-carrying MtaC subunits is investigated and the 2.5-Å crystal structure of this complex organized as a (MtaBC)2 heterotetramer is reported.
Abstract: Some methanogenic and acetogenic microorganisms have the catalytic capability to cleave heterolytically the CO bond of methanol. To obtain insight into the elusive enzymatic mechanism of this challenging chemical reaction we have investigated the methanol-activating MtaBC complex from Methanosarcina barkeri composed of the zinc-containing MtaB and the 5-hydroxybenzimidazolylcobamide-carrying MtaC subunits. Here we report the 2.5-Å crystal structure of this complex organized as a (MtaBC)2 heterotetramer. MtaB folds as a TIM barrel and contains a novel zinc-binding motif. Zinc(II) lies at the bottom of a funnel formed at the C-terminal β-barrel end and ligates to two cysteinyl sulfurs (Cys-220 and Cys-269) and one carboxylate oxygen (Glu-164). MtaC is structurally related to the cobalamin-binding domain of methionine synthase. Its corrinoid cofactor at the top of the Rossmann domain reaches deeply into the funnel of MtaB, defining a region between zinc(II) and the corrinoid cobalt that must be the binding site for methanol. The active site geometry supports a SN2 reaction mechanism, in which the CO bond in methanol is activated by the strong electrophile zinc(II) and cleaved because of an attack of the supernucleophile cob(I)amide. The environment of zinc(II) is characterized by an acidic cluster that increases the charge density on the zinc(II), polarizes methanol, and disfavors deprotonation of the methanol hydroxyl group. Implications of the MtaBC structure for the second step of the reaction, in which the methyl group is transferred to coenzyme M, are discussed.

113 citations

Journal ArticleDOI
TL;DR: The extent of isotopic fractionation between the carbon substrate and the products of M. barkeri was dependent on the substrate type and availability, and the 13 C content of lipids varied with substrate availability in some cases, but did not show patterns that could be used to identify the growth substrate of methanogens in natural environments.

113 citations

Journal ArticleDOI
TL;DR: A strong protective environment was afforded to the methanogens against heavy metal toxicity in the sludge, indicating a strong protective environments was afforded the metanobacterium against heavyMetal toxicity inThe sludge.
Abstract: The effect of ammonium chloride, sodium butyrate, sodium propionate, and the heavy metals nickel, zinc, and copper on methanogenesis by pure cultures of Methanospirillum hungatei, Methanosarcina ba...

113 citations

Journal ArticleDOI
TL;DR: Key amino acid residues identified genetically in the E. coli enzyme were conserved in the methanogenic enzyme, which suggests that vacuolar, F1, meetinghanogenic, and S. acidocaldarius ATPases were derived from a common ancestral enzyme.

112 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20237
202212
202112
202012
20197
201818