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Literature summary for 2.8.4.1 extracted from

  • Dey, M.; Kunz, R.C.; Lyons, D.M.; Ragsdale, S.W.
    Characterization of alkyl-nickel adducts generated by reaction of methyl-coenzyme M reductase with brominated acids (2007), Biochemistry, 46, 11969-11978.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.8.4.1

Inhibitors

Inhibitors Comment Organism Structure
3-bromopropane sulfonate BPS, forms an alkyl-Ni(III) species with MCRred1is that elicits the MCRPS EPR signal; irreversible inhibition Methanothermobacter marburgensis
4-bromobutane sulfonate when reacted with 4-bromobutyrate, MCRred1 forms the alkyl-Ni(III) MCRXA state and then self-reactivation to regenerate the Ni(I) MCRred1 state and a bromocarboxy ester Methanothermobacter marburgensis
bromopropionate
-
 Methanothermobacter marburgensis
additional information inhibition mechanism, brominated carboxylic acids, with carbon chain lengths of 4-16, all give rise to an alkyl-Ni intermediate with an EPR signal similar to that of the MCRPS species, brominated carboxylic acids mimic the interactions of BPS and methyl-SCoM at the MCR active site, overview Methanothermobacter marburgensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics of MCRred1 with brominated acids, overview Methanothermobacter marburgensis
additional information
-
 additional information transient kinetics study, overview Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CH3-S-CoM + HS-CoB Methanothermobacter marburgensis i.e. methyl-coenzyme M + coenzyme B CoM-S-S-CoB + methane
-
 ?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Methanothermobacter marburgensis i.e. methyl-SCoM methane + CoB-S-S-CoM a the mixed disulfide ?
additional information Methanothermobacter marburgensis MCR catalyzes the final step in the biological synthesis of methane. Using coenzyme B, CoBSH, as the two-electron donor, MCR reduces methyl-coenzyme M, methyl-SCoM, to methane and the mixed disulfide, CoB-S-S-CoM. MCR contains coenzyme F430, an essential redox-active nickel tetrahydrocorphin, at its active site. The active form of MCR, MCRred1, contains Ni(I)-F430 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
methyl-CoM + CoB = CoM-S-S-CoB + methane mechanism, nucleophilic attack of Ni(I)-MCRred1 on the methyl group of methyl-SCoM generates a methyl-Ni intermediate Methanothermobacter marburgensis
a
methyl-CoM + CoB = CoM-S-S-CoB + methane Two reaction mechanisms for methane formation distinguishable by the first step of catalysis, overview Methanothermobacter marburgensis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CH3-S-CoM + HS-CoB i.e. methyl-coenzyme M + coenzyme B Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?
CH3-S-CoM + HS-CoB i.e. methyl-coenzyme M + coenzyme B, selectivity of the MCR reaction toward nucleophilic attack by Ni(I) Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanothermobacter marburgensis methane + CoM-S-S-CoB a the mixed disulfide ?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanothermobacter marburgensis methane + CoB-S-S-CoM a the mixed disulfide ?
methylmercaptopropionate + HS-CoB is about 110fold less reactive than the natural substrate methyl-SCoM Methanothermobacter marburgensis ?
-
 ?
additional information the enzyme performs reactions with brominated acid, 4-bromobutyric acid to 16-bromohexadecanoic acid, analogously to the reaction of MCRred1, the active Ni(I)-F430 containing enzyme form, to generate a methyl-Ni(III) intermediate in methane formation with the natural substrate, methyl-SCoM, substrate specificity and acivities, overview Methanothermobacter marburgensis ?
-
 ?
additional information MCR catalyzes the final step in the biological synthesis of methane. Using coenzyme B, CoBSH, as the two-electron donor, MCR reduces methyl-coenzyme M, methyl-SCoM, to methane and the mixed disulfide, CoB-S-S-CoM. MCR contains coenzyme F430, an essential redox-active nickel tetrahydrocorphin, at its active site. The active form of MCR, MCRred1, contains Ni(I)-F430 Methanothermobacter marburgensis ?
-
 ?

Synonyms

Synonyms Comment Organism
MCR
-
 Methanothermobacter marburgensis
methyl-coenzyme M reductase
-
 Methanothermobacter marburgensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Methanothermobacter marburgensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
coenzyme F430 an essential redox-active nickel tetrahydrocorphin, bound at the active site, the active form of MCR, MCRred1, contains Ni(I)-F430 Methanothermobacter marburgensis
F-430 with Ni(I) oxidation state, selectivity of the MCR reaction toward nucleophilic attack by Ni(I) Methanothermobacter marburgensis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00005
-
 3-bromopropane sulfonate
-
 Methanothermobacter marburgensis