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Journal ArticleDOI

Do corrinoids function in the methanogenic dissimilation of methanol by Methanosarcina barkeri

S. Shapiro
- 01 Jun 1982 - 
- Vol. 28, Iss: 6, pp 629-635
TLDR
Results indicate that methylcobalamin-HS-CoM methyl-transferase is not involved in the biosynthesis of CH3-S- CoM or CH4 from CH3OH by M. barkeri.
Abstract
The participation of corrinoids in the biosynthesis of CH3-S-CoM and CH4 from CH3OH by extracts of heterotrophically and autotrophically grown cells of Methanosarcina barkeri was investigated. Alkyl-B12 derivatives severely inhibited the transfer of the Co-methyl moiety of CH3-B12 to HS-CoM, but hardly affected the formation of CH3-S-CoM and CH4 from CH3OH. 1-Iodoalkanes completely suppressed methanogenesis from CH3OH, but only slightly inhibited the biosynthesis of CH3-S-CoM. Additionally, [methyl-3H]methylcobalamin could not be detected in cell-free extracts following biosynthesis of [methyl-3H]CH3-S-CoM from HS-CoM and excess [methyl-3H]CH3OH. These results indicate that methylcobalamin-HS-CoM methyl-transferase is not involved in the biosynthesis of CH3-S-CoM or CH4 from CH3OH by M. barkeri.

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Citations
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Journal ArticleDOI

The bioenergetics of methanogenesis.

TL;DR: The reduction of CO2 or any other methanogenic substrate to methane serves the same function as the reduction of oxygen, nitrate or sulfate to more reduced products and these exergonic reactions are coupled to the production of usable energy generated through a charge separation and a protonmotive-force-driven ATPase.
Journal ArticleDOI

The acetyl-CoA pathway of autotrophic growth

TL;DR: It is concluded that the formation of acetyl-CoA by other acetogens, the methanogens and sulphate-reducing bacteria occurs by a mechanism very similar to that of C. thermoaceticum.
Journal ArticleDOI

Methyltransferases involved in methanol conversion by Methanosarcina barkeri.

TL;DR: The enzyme system involved in the methyltransfer from methanol to 2-mercaptoethanesulfonate (HS-CoM) was resolved into two enzyme fractions and one enzyme appears to be a cobalamin-containing protein, which is oxygen sensitive.
Journal ArticleDOI

Electron transfer reactions in methanogens

TL;DR: Intermediary cell carbon synthesis starting from acetyl-CoA involves reductive carboxylations and oxidoreductions by the participation of the enzymes of the tricarboxylic acid cycle.
Book ChapterDOI

Conversion of Methanol and Methylamines to Methane and Carbon Dioxide

TL;DR: Biochemically, M. barkeri is the best studied methylotrophic methanogen and most of the work reviewed in this chapter refers to it.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter

TL;DR: A modification of the naphthalene-dioxane-PPO liquid scintillator has been described which will allow up to 3.0 ml of an aqueous solution to be counted as mentioned in this paper.
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Methanobacillus omelianskii, a Symbiotic Association of Two Species of Bacteria*

TL;DR: The results indicate that M. omelianskii maintained in ethanol media is actually a symbiotic association of the two species.
Journal ArticleDOI

Structure and Methylation of Coenzyme M (HSCH2CH2SO3)

TL;DR: Coenzyme M is a recently discovered cofactor which is involved in methyl transfer reactions in Methanobacterium and evidence indicates that an active form of this cofactor is 2-mercaptoethanesulfonic acid which is methylated producing 2-(methylthio) ethanesulfonics acid.
Journal ArticleDOI

Fermentation of glucose, fructose, and xylose by Clostridium thermoaceticum: effect of metals on growth yield, enzymes, and the synthesis of acetate from CO 2

TL;DR: Clostridium thermoaceticum ferments xylose, fructose, and glucose with acetate as the only product, and the following enzymes involved in the synthesis of acetate from CO(2) and in the metabolism of pyruvate are present in extracts.
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