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The taxonomic range for the selected organisms is: Methanothermobacter marburgensis
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
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2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
2-(methylthio)ethansulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
-
i.e. CoM and CoB
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
CH3-S-CoM + HS-CoB6
CoM-S-S-CoB6 + methane
-
i.e. N-7-mercaptohexanoylthreonine phosphate
-
-
?
CH3-S-CoM + HS-CoB8
CoM-S-S-CoB8 + methane
-
a two-electron transfer reaction
-
-
?
CH3-S-CoM + HS-CoB9
CoM-S-S-CoB9 + methane
-
-
-
-
?
CH3-S-CoM + SH-CoB
CoM-S-S-CoB + methane
-
-
-
-
?
CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
CH3-S-CoM + SH-CoB6
CoM-S-S-CoB6 + methane
CH3-S-CoM + SH-CoB8
CoM-S-S-CoB8 + methane
i.e. N-8-mercaptooctanoylthreonine phosphate
-
-
?
CH3-S-CoM + SH-CoB9
CoM-S-S-CoB9 + methane
i.e. N-9-mercaptononanoylthreonine phosphate
-
-
?
CH3-S-CoM3 + HS-CoB8
CoM3-S-S-CoB8 + methane
-
-
-
-
?
ethyl coenzyme M + coenzyme B
ethane + CoM-S-S-CoB
-
1% of the activity with methyl coenzyme M
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoB-S-S-CoM
-
i.e. methyl-SCoM
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
methyl-CoM + CoB
CoM-S-S-CoB + methane
methylmercaptopropionate + HS-CoB
?
-
is about 110fold less reactive than the natural substrate methyl-SCoM
-
-
?
additional information
?
-
2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
-
i.e. CoM and CoB
-
-
?
2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate
CoM-S-S-CoB + methane
-
i.e. CoM and CoB, the enzyme exists in the the inactive Ni(II) MCRox1-silent form and the active Ni(I) MCRred1 form with transition from MCRred1 to MCRred2 forms, the protein is able to undergo a conformational change upon binding of the second substrate. Analysis of the catalytic mechanism of the reduction at the nickel center using inhibitory fluorescent trifluoromethyl thio esters of the substrate CoB for spectroscopic analysis of the structure of the enzyme-cofactor complex, derivatives synthesis, overview
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
-
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
i.e. methyl-coenzyme M + coenzyme B
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
key step in the convertion of C1 substrates or acetate to methane thereby providing energy for the cell
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
MCR catalyzes the first proposed step in anaerobic methane oxidation and terminal step in methanogenesis by using N-7-mercaptoheptanolyl-threonine phosphate, i.e. CoB-SH. as the two-electron donor to reduce 2-(methylthiol)-ethane sulfonate, i.e. methyl-SCoM, to methane, and producing the heterodisulfide, CoBS-SCoM
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
MCR catalyzes the methane-forming step in methanogenic archaea
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
catalytic cycle and proton transfer mechanism and energetics, reaction complex formations and mechanism, detailed overview
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
i.e. methyl-coenzyme M + coenzyme B, selectivity of the MCR reaction toward nucleophilic attack by Ni(I)
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
i.e. methyl-coenzyme M or 2-methylmercaptoethanesulfonate + coenzyme B or N-7-mercaptoheptanoylthreonine phosphate
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
the active enzyme is in the MCRred1c form, coordinated ligands of the two paramagnetic MCRred2 states, reduction and oxidation states and critical bond activation step, detailed overview
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
HS-CoB is N-(7-mercaptoheptanoyl)-L-threonine 3-O-phosphate
-
-
?
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
-
i.e. N-7-mercaptoheptanoylthreonine phosphate, Ni(III)-methyl is an intermediate in methane formation
-
-
?
CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
-
-
-
-
?
CH3-S-CoM + SH-CoB5
CoM-S-S-CoB5 + methane
i.e. N-5-mercaptopentanoylthreonine phosphate
-
-
?
CH3-S-CoM + SH-CoB6
CoM-S-S-CoB6 + methane
i.e. N-6-mercaptohexanoylthreonine phosphate, slow substrate
-
-
?
CH3-S-CoM + SH-CoB6
CoM-S-S-CoB6 + methane
-
methanogenesis occurs 1000fold more slowly than with SH-CoB
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
-
?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
discussion of mechanism
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
-
-
-
?
methyl-coenzyme M + coenzyme B
methane + CoM-S-S-CoB
-
spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase
-
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
i.e. methyl-SCoM
a the mixed disulfide
-
?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
-
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
?
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
-
r
methyl-CoM + CoB
CoM-S-S-CoB + methane
-
-
-
?
additional information
?
-
-
MCR also appears to initiate anaerobic methane oxidation, the reverse methanogenesis
-
-
?
additional information
?
-
-
the enzyme catalyzes the final step in methane biosynthesis by methanogenic archaea
-
-
?
additional information
?
-
-
the enzyme catalyzes the formation of methane from methyl-coenzyme M and coenzyme B in methanogenic archaea
-
-
?
additional information
?
-
-
conversion of MCRox1 toMCRred1 by Ti(III)citrate, bromopropanesulfonate is an alternative substrate of MCR in an ionic reaction that is coenzyme B-independent and leads to debromination of bromopropanesulfonate and formation of a distinct state with an EPR signal that is assigned to a Ni(III)-propylsulfonate species, propanesulfonate formation also occurs in steady-state reactions in the presence of Ti(III) citrate
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
MCR reduction/oxidation state, electron paramagnetic resonance status analysis, detailed overview
-
-
?
additional information
?
-
-
MCR substrate specificity and reactivation activity of different thiols, e.g. 2-mercaptoethanol, DTT, Na2S, and cysteine, kinetics, overview
-
-
?
additional information
?
-
-
three general mechanisms for the catalytic production of methane by MCR: (1) the Ni-Me/Ragsdale pathway, (2) the Ni-Me/Thauer pathway, (3) the methyl radical pathway. Density functional calculations and electronic-structure calculations and analysis by computational methods, homolytic Ni-S/Ni-C bonds energies, overview
-
-
?
additional information
?
-
-
MCR is the key enzyme in methane formation by methanogenic Archaea. It converts the thioether methyl-coenzyme M and the thiol coenzyme B into methane and the heterodisulfide of coenzyme M and coenzyme B
-
-
?
additional information
?
-
-
The active form of the enzyme, referred to as MCRred1, features the tetracoordinate dx2y2 nickel(I) state of the cofactor, simulations of enzyme nickel intermediate states in synthetic complexes, mechanism and modeling, pyriporphyrin-based model and isoporphyrin-based model, overview
-
-
?
additional information
?
-
-
no activity with SH-CoB8 or SH-CoB9
-
-
?
additional information
?
-
the substrates bind inside a deep substrate channel with CoBSH nearer to the surface, stretching toward methyl-SCoM, which is close to F430
-
-
-
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coenzyme F430
-
-
coenzyme F430
-
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
coenzyme F430
-
a redox-active nickel tetrahydrocorphin bound at the active site, contains low-spin Ni(II), determination of the cofactor reduction site at the exocyclic ketone group by NMR study, mass spectrometry, and QM/MM computations, conversion of F430 to F330 reduces the hydrocorphin ring but not the metal, reduction of F430 with Ti(III) citrate to generate F380, corresponding to the active MCRred1 state, reduces the Ni(II) to Ni(I) but does not reduce the tetrapyrrole ring system, overview
coenzyme F430
-
an essential redox-active nickel tetrahydrocorphin, bound at the active site, the active form of MCR, MCRred1, contains Ni(I)-F430
coenzyme F430
-
each active site has the nickel porphyrinoid F430 as a prosthetic group, in the active state, F430 contains the transition metal in the Ni(I) oxidation state
coenzyme F430
-
the nickel-containing tetrapyrrole is essential for the reaction, and is bound to the active site
F-430
-
-
F-430
-
cofactor F430 undergoes a significant conformational change when it binds to the enzyme. Conversion from MCRox1 to MCRred1 involves major conformational rearrangements, which are propose to be due to a 2-electron reversible reduction of the hydrocorphin ring of F430
F-430
-
nickel-containing porphinoid cofactor F-430. Comparison of the free cofactor in the (+)1, (+)2 and (+)3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms
F-430
-
prosthetic group has to be in the Ni(I) oxidation state for the enzyme to be active
F-430
-
tightly bound nickel porphinol. The enzyme is active only when its prosthetic group in in the NI(I)-reduced state
F-430
-
active in Ni(I) oxidation state, inactive in Ni(II) state, binding structure and oxidation states, hyperfine interactions of protons, detailed overview
F-430
-
binding structure, and different oxidation states F430 (Ni(I)/Ni(II)/Ni(III)), Ni(I) is the active state, overview
F-430
-
the active site of MCR includes a noncovalently bound Ni tetrapyrrolic coenzyme F430, which is in the Ni(I) state in the active enzyme, MCRred1
F-430
-
the enzyme has two structurally interlinked active sites embedded in an alpha2beta2gamma2 subunit structure. Each active site has the nickel porphyrinoid F430 as a prosthetic group. In the active state, F430 contains the transition metal in the Ni(I) oxidation state
F-430
-
with Ni(I) oxidation state
F-430
-
with Ni(I) oxidation state, selectivity of the MCR reaction toward nucleophilic attack by Ni(I)
F-430
-
a nickel hydrocorphin coenzyme F430, the Ni(I) MCRred1 form and the inactive Ni(II) MCRox1-silent form, no formation of an MCRis dependent methyl-Ni(F430) species, analysis of the catalytic mechanism of the reduction at the nickel center using inhibitory fluorescent trifluoromethyl thio esters of the substrate CoB for spectroscopic analysis of the structure of the enzyme-cofactor complex, derivatives synthesis, overview
F-430
-
an active site Ni cofactor
F-430
-
the Ni-F430 cofactor is bound to the active site and exists in two oxidation states
F-430
-
the active site of the enzyme contains an essential redox-active nickel tetrapyrrole cofactor, coenzyme F430, which is active in the Ni(I) state
F-430
the enzyme contains the highly reduced nickel-tetrapyrrole coenzyme F430
F-430
coenzyme F430, rapid kinetic studies rule out methyl-Ni(III) and trap the MCRox1-silent intermediate. Identification of an MCRox1-like state, specifically a F430-Ni(III)-SCoM/CoBS- intermediate, from direct DFT calculations
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Ermler, U.
On the mechanism of methyl-coenzyme M reductase
Dalton Trans.
2005
3451-3458
2005
Methanothermobacter marburgensis
brenda
Tang, Q.; Carrington, P.E.; Horng, Y.C.; Maroney, M.J.; Ragsdale, S.W.; Bocian, D.F.
X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation
J. Am. Chem. Soc.
124
13242-13256
2002
Methanothermobacter marburgensis
brenda
Harmer, J.; Finazzo, C.; Piskorski, R.; Bauer, C.; Jaun, B.; Duin, E.C.; Goenrich, M.; Thauer, R.K.; Van Doorslaer, S.; Schweiger, A.
Spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase: A Pulse EPR Study
J. Am. Chem. Soc.
127
17744-17755
2005
Methanothermobacter marburgensis
brenda
Goenrich, M.; Duin, E.C.; Mahlert, F.; Thauer, R.K.
Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B
J. Biol. Inorg. Chem.
10
333-342
2005
Methanothermobacter marburgensis
brenda
Mahlert, F.; Grabarse, W.; Kahnt, J.; Thauer, R.K.; Duin, E.C.
The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states
J. Biol. Inorg. Chem.
7
101-112
2002
Methanothermobacter marburgensis
brenda
Mahlert, F.; Bauer, C.; Jaun, B.; Thauer, R.K.; Duin, E.C.
The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2
J. Biol. Inorg. Chem.
7
500-513
2002
Methanothermobacter marburgensis
brenda
Duin, E.C.; Signor, L.; Piskorski, R.; Mahlert, F.; Clay, M.D.; Goenrich, M.; Thauer, R.K.; Jaun, B.; Johnson, M.K.
Spectroscopic investigation of the nickel-containing porphinoid cofactor F(430). Comparison of the free cofactor in the (+)1, (+)2 and (+)3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms
J. Biol. Inorg. Chem.
9
563-576
2004
Methanothermobacter marburgensis
brenda
Goenrich, M.; Mahlert, F.; Duin, E.C.; Bauer, C.; Jaun, B.; Thauer, R.K.
Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues
J. Biol. Inorg. Chem.
9
691-705
2004
Methanothermobacter marburgensis
brenda
Dey, M.; Kunz, R.C.; Van Heuvelen, K.M.; Craft, J.L.; Horng, Y.C.; Tang, Q.; Bocian, D.F.; George, S.J.; Brunold, T.C.; Ragsdale, S.W.
Spectroscopic and computational studies of reduction of the metal versus the tetrapyrrole ring of coenzyme F430 from methyl-coenzyme M reductase
Biochemistry
45
11915-11933
2006
Methanothermobacter marburgensis
brenda
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
Biochemistry
46
11969-11978
2007
Methanothermobacter marburgensis
brenda
Kahnt, J.; Buchenau, B.; Mahlert, F.; Krueger, M.; Shima, S.; Thauer, R.K.
Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea
FEBS J.
274
4913-4921
2007
Methanocaldococcus jannaschii, Methanococcus voltae, Methanoculleus thermophilus, Methanopyrus kandleri, Methanopyrus kandleri (Q49605), Methanosarcina barkeri, Methanothermobacter marburgensis
brenda
Kunz, R.C.; Horng, Y.C.; Ragsdale, S.W.
Spectroscopic and kinetic studies of the reaction of bromopropanesulfonate with methyl-coenzyme M reductase
J. Biol. Chem.
281
34663-34676
2006
Methanothermobacter marburgensis
brenda
Kern, D.I.; Goenrich, M.; Jaun, B.; Thauer, R.K.; Harmer, J.; Hinderberger, D.
Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy
J. Biol. Inorg. Chem.
12
1097-1105
2007
Methanothermobacter marburgensis
brenda
Kunz, R.C.; Dey, M.; Ragsdale, S.W.
Characterization of the thioether product formed from the thiolytic cleavage of the alkyl-nickel bond in methyl-coenzyme M reductase
Biochemistry
47
2661-2667
2008
Methanothermobacter marburgensis
brenda
Harmer, J.; Finazzo, C.; Piskorski, R.; Ebner, S.; Duin, E.C.; Goenrich, M.; Thauer, R.K.; Reiher, M.; Schweiger, A.; Hinderberger, D.; Jaun, B.
A nickel hydride complex in the active site of methyl-coenzyme M reductase: implications for the catalytic cycle
J. Am. Chem. Soc.
130
10907-10920
2008
Methanothermobacter marburgensis
brenda
Hinderberger, D.; Ebner, S.; Mayr, S.; Jaun, B.; Reiher, M.; Goenrich, M.; Thauer, R.K.; Harmer, J.
Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase
J. Biol. Inorg. Chem.
13
1275-1289
2008
Methanothermobacter marburgensis
brenda
Duin, E.C.; McKee, M.L.
A new mechanism for methane production from methyl-coenzyme M reductase as derived from density functional calculations
J. Phys. Chem. B
112
2466-2482
2008
Methanothermobacter marburgensis
brenda
Sarangi, R.; Dey, M.; Ragsdale, S.W.
Geometric and electronic structures of the Ni(I) and methyl-Ni(III) intermediates of methyl-coenzyme M reductase
Biochemistry
48
3146-3156
2009
Methanothermobacter marburgensis
brenda
Gonzalez, E.; Ghosh, A.
Models of the ox1 state of methylcoenzyme M reductase: where are the electrons?
Chemistry
14
9981-9989
2008
Methanothermobacter marburgensis
brenda
Ebner, S.; Jaun, B.; Goenrich, M.; Thauer, R.K.; Harmer, J.
Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase
J. Am. Chem. Soc.
132
567-575
2010
Methanothermobacter marburgensis
brenda
Wrede, C.; Walbaum, U.; Ducki, A.; Heieren, I.; Hoppert, M.
Localization of methyl-coenzyme M reductase as metabolic marker for diverse methanogenic Archaea
Archaea
2013
920241
2013
Methanococcus maripaludis, Methanococcus maripaludis DSM 2067, Methanosarcina mazei, Methanosarcina mazei DSM 3318, Methanosarcina mazei DSM 3647, Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133, Methanothermobacter wolfeii, Methanothermobacter wolfeii DSM 2970
brenda
Dey, M.; Li, X.; Kunz, R.C.; Ragsdale, S.W.
Detection of organometallic and radical intermediates in the catalytic mechanism of methyl-coenzyme M reductase using the natural substrate methyl-coenzyme M and a coenzyme B substrate analogue
Biochemistry
49
10902-10911
2010
Methanothermobacter marburgensis, Methanothermobacter marburgensis OCM82
brenda
Cedervall, P.E.; Dey, M.; Pearson, A.R.; Ragsdale, S.W.; Wilmot, C.M.
Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues
Biochemistry
49
7683-7693
2010
Methanothermobacter marburgensis (P11558 and P11560 and P11562), Methanothermobacter marburgensis OCM82 (P11558 and P11560 and P11562)
brenda
Cedervall, P.E.; Dey, M.; Li, X.; Sarangi, R.; Hedman, B.; Ragsdale, S.W.; Wilmot, C.M.
Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis
J. Am. Chem. Soc.
133
5626-5628
2011
Methanothermobacter marburgensis
brenda
Wagner, T.; Kahnt, J.; Ermler, U.; Shima, S.
Didehydroaspartate modification in methyl-coenzyme M reductase catalyzing methane formation
Angew. Chem. Int. Ed. Engl.
55
10630-10633
2016
Methanosarcina barkeri, Methanothermobacter wolfeii, Methanothermobacter marburgensis
brenda
Wongnate, T.; Ragsdale, S.W.
The reaction mechanism of methyl-coenzyme M reductase: how an enzyme enforces strict binding order
J. Biol. Chem.
290
9322-9334
2015
Methanothermobacter marburgensis
brenda
Su, J.; Yang, X.; He, J.; Zhang, Y.; Duan, X.; Wang, R.; Shen, W.
Methyl-coenzyme M reductase-dependent endogenous methane enhances plant tolerance against abiotic stress and alters ABA sensitivity in Arabidopsis thaliana
Plant Mol. Biol.
101
439-454
2019
Methanothermobacter marburgensis (P11558 and P11560 and P11562), Methanothermobacter marburgensis Marburg (P11558 and P11560 and P11562), Methanothermobacter marburgensis ATCC BAA-927 (P11558 and P11560 and P11562), Methanothermobacter marburgensis NBRC 100331 (P11558 and P11560 and P11562), Methanothermobacter marburgensis JCM 14651 (P11558 and P11560 and P11562), Methanothermobacter marburgensis DSM 2133 (P11558 and P11560 and P11562), Methanothermobacter marburgensis OCM 82 (P11558 and P11560 and P11562)
brenda
Arokiyaraj, S.; Stalin, A.; Shin, H.
Anti-methanogenic effect of rhubarb (Rheum spp.) - an in silico docking studies on methyl-coenzyme M reductase (MCR)
Saudi J. Biol. Sci.
26
1458-1462
2019
Methanothermobacter marburgensis
brenda
Wongnate, T.; Sliwa, D.; Ginovska, B.; Smith, D.; Wolf, M.W.; Lehnert, N.; Raugei, S.; Ragsdale, S.W.
The radical mechanism of biological methane synthesis by methyl-coenzyme M reductase
Science
352
953-958
2016
Methanothermobacter marburgensis (P11558 and P11560 and P11562)
brenda