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Merck

50187

Sigma-Aldrich

Ammonium 2-(methylthio)ethanesulfonate

≥97.0% (TLC)

Sinónimos:

Methyl coenzyme M ammonium salt

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About This Item

Fórmula empírica (notación de Hill):
C3H11NO3S2
Número de CAS:
Peso molecular:
173.25
Número MDL:
Código UNSPSC:
12352106
ID de la sustancia en PubChem:
NACRES:
NA.25

Ensayo

≥97.0% (TLC)

cadena SMILES

N.CSCCS(O)(=O)=O

InChI

1S/C3H8O3S2.H3N/c1-7-2-3-8(4,5)6;/h2-3H2,1H3,(H,4,5,6);1H3

Clave InChI

FSGSBLDVKBYXIK-UHFFFAOYSA-N

Aplicación

Ammonium 2-(methylthio)ethanesulfonate (Methyl coenzyme M) is converted into methane by the enzyme Methyl-coenzyme M reductase (MCR) derived from methanogenic archaea. Methy-coenzyme M is used in studies on methanogenic (methane-producing) enzymatic processes.

Envase

Bottomless glass bottle. Contents are inside inserted fused cone.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Corinne Biderre-Petit et al.
FEMS microbiology ecology, 77(3), 533-545 (2011-05-21)
Lake Pavin is a meromictic crater lake located in the French Massif Central area. In this ecosystem, most methane (CH(4)) produced in high quantity in the anoxic bottom layers, and especially in sediments, is consumed in the water column, with
D A Grahame et al.
Biochemical and biophysical research communications, 147(1), 254-258 (1987-08-31)
Buffer-soluble extracts of acetate-grown Methanosarcina barkeri catalyzed methanogenesis from acetate in the presence of hydrogen and ATP. The rates of methane formation from either acetate plus ATP, or acetylphosphate without ATP added, were approximately doubled by the addition of coenzyme
L G Bonacker et al.
European journal of biochemistry, 217(2), 587-595 (1993-10-15)
Methyl-coenzyme M reductase (MCR) catalyses the methane-forming step in the energy metabolism of methanogenic Archaea. It brings about the reduction of methyl-coenzyme M (CH3-S-CoM) by 7-mercaptoheptanoylthreonine phosphate (H-S-HTP). Methanobacterium thermoautotrophicum contains two isoenzymes of MCR, designated MCR I and MCR
K D Olson et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(10), 4099-4103 (1991-05-15)
Inactive 2-(methylthio)ethanesulfonic acid (CH3-S-CoM) reductase was partially activated by exposure to light. This simplified system replaces the complex enzymatic system of protein components A2, A3a, A3b, and ATP, which previously represented the only available means of reactivating the enzyme. Components
U Ermler et al.
Science (New York, N.Y.), 278(5342), 1457-1462 (1997-12-31)
Methyl-coenzyme M reductase (MCR), the enzyme responsible for the microbial formation of methane, is a 300-kilodalton protein organized as a hexamer in an alpha2beta2gamma2 arrangement. The crystal structure of the enzyme from Methanobacterium thermoautotrophicum, determined at 1.45 angstrom resolution for

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