50187
Ammonium-2-(methylthio)ethansulfonat Ammoniumsalz
≥97.0% (TLC)
Synonym(e):
Methyl-coenzym M Ammoniumsalz
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About This Item
Empirische Formel (Hill-System):
C3H11NO3S2
CAS-Nummer:
Molekulargewicht:
173.25
MDL-Nummer:
UNSPSC-Code:
12352106
PubChem Substanz-ID:
NACRES:
NA.25
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Assay
≥97.0% (TLC)
SMILES String
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
InChIKey
FSGSBLDVKBYXIK-UHFFFAOYSA-N
Anwendung
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.
Verpackung
Bottomless glass bottle. Contents are inside inserted fused cone.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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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
J T Keltjens et al.
European journal of biochemistry, 172(2), 471-476 (1988-03-01)
Cell-free extracts of Methanobacterium thermoautotrophicum (strain delta H) were found to contain high concentrations of inorganic pyrophosphate (up to 40 mM). The compound was accumulated by the organism despite high activity of inorganic pyrophosphatase which was found to be present
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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