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Article: Enzymology. Nickel to the fore.

Thauer, R K

2001 Volume 293, Issue 5533, Page(s) 1264–1265

MeSH term(s)	Aldehyde Oxidoreductases/chemistry ; Aldehyde Oxidoreductases/genetics ; Aldehyde Oxidoreductases/metabolism ; Bacteria, Anaerobic/enzymology ; Binding Sites ; Carbon Monoxide/metabolism ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Electron Transport ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Iron/chemistry ; Iron/metabolism ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/genetics ; Multienzyme Complexes/metabolism ; Nickel/chemistry ; Nickel/metabolism ; Oxidation-Reduction ; Peptococcaceae/enzymology ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Sulfur/chemistry
Chemical Substances	Multienzyme Complexes ; Recombinant Proteins ; Sulfur (70FD1KFU70) ; Nickel (7OV03QG267) ; Carbon Monoxide (7U1EE4V452) ; Iron (E1UOL152H7) ; Aldehyde Oxidoreductases (EC 1.2.-) ; carbon monoxide dehydrogenase (EC 1.2.7.4)
Language	English
Publishing date	2001-08-15
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.1064049
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Article: Ferredoxin-dependent methane formation from acetate in cell extracts of Methanosarcina barkeri (strain MS).

Fischer, R / Thauer, R K

FEBS letters

2004 Volume 269, Issue 2, Page(s) 368–372

Abstract: Cell extracts of Methanosarcina barkeri grown on acetate catalyzed the conversion of acetyl-CoA to CO2 and CH4 at a specific rate of 50 nmol min-1 mg-1. When ferredoxin was removed from the extracts by DEAE-Sephacel anion exchange chromatography, the ... ...

Abstract	Cell extracts of Methanosarcina barkeri grown on acetate catalyzed the conversion of acetyl-CoA to CO2 and CH4 at a specific rate of 50 nmol min-1 mg-1. When ferredoxin was removed from the extracts by DEAE-Sephacel anion exchange chromatography, the extracts were inactive but full activity was restored upon addition of purified ferredoxin from M. barkeri or from Clostridium pasteurianum. The apparent Km for ferredoxin from M. barkeri was determined to be 2.5 M. A ferredoxin dependence was also found for the formation of CO2, H2 and methylcoenzyme M from acetyl-CoA, when methane formation was inhibited by bromoethanesulfonate. Reduction of methyl-coenzyme M with H2 did not require ferredoxin. These and other data indicate that ferredoxin is involved as electron carrier in methanogenesis from acetate. Methanogenesis from acetyl-CoA in cell extracts was not dependent on the membrane fraction, which contains the cytochromes.
MeSH term(s)	Acetates/chemistry ; Acetates/metabolism ; Acetyl Coenzyme A/chemistry ; Acetyl Coenzyme A/metabolism ; Cell Extracts ; Ferredoxins/chemistry ; Ferredoxins/metabolism ; Methane/chemistry ; Methane/metabolism ; Methanosarcina barkeri/chemistry ; Methanosarcina barkeri/metabolism
Chemical Substances	Acetates ; Cell Extracts ; Ferredoxins ; Acetyl Coenzyme A (72-89-9) ; Methane (OP0UW79H66)
Language	English
Publishing date	2004-06-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/0014-5793(90)81195-t
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Article: Hollow carbon sphere/metal oxide nanocomposites anodes for lithium-ion batteries

Wenelska, K / A. Ottmann / E. Mijowska / E. Thauer / P. Schneider / R. Klingeler

Energy. 2016 May 15, v. 103

2016

Abstract: HCS (Hollow carbon spheres) covered with metal oxide nanoparticles (SnO2 and MnO2, respectively) were successfully synthesized and investigated regarding their potential as anode materials for lithium-ion batteries. Raman spectroscopy shows a high degree ...

Abstract	HCS (Hollow carbon spheres) covered with metal oxide nanoparticles (SnO2 and MnO2, respectively) were successfully synthesized and investigated regarding their potential as anode materials for lithium-ion batteries. Raman spectroscopy shows a high degree of graphitization for the HCS host structure. The mesoporous nature of the nanocomposites is confirmed by Brunauer–Emmett–Teller analysis. For both metal oxides under study, the metal oxide functionalization of HCS yields a significant increase of electrochemical performance. The charge capacity of HCS/SnO2 is 370 mA hg−1 after 45 cycles (266 mA hg−1 in HCS/MnO2) which clearly exceeds the value of 188 mA hg−1 in pristine HCS. Remarkably, the data imply excellent long term cycling stability after 100 cycles in both cases. The results hence show that mesoporous HCS/metal oxide nanocomposites enable exploiting the potential of metal oxide anode materials in Lithium-ion batteries by providing a HCS host structure which is both conductive and stable enough to accommodate big volume change effects.
Keywords	anodes ; carbon ; electrochemistry ; lithium batteries ; manganese dioxide ; nanocomposites ; nanoparticles ; porous media ; Raman spectroscopy ; tin dioxide
Language	English
Dates of publication	2016-0515
Size	p. 100-106.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	2019804-8
ISSN	0360-5442 ; 0360-5442
ISSN (online)	0360-5442
ISSN	0360-5442
DOI	10.1016/j.energy.2016.02.063
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Article ; Online: Methyl-coenzyme M reductase from methanogenic archaea: isotope effects on label exchange and ethane formation with the homologous substrate ethyl-coenzyme M.

Scheller, Silvan / Goenrich, Meike / Thauer, Rudolf K / Jaun, Bernhard

Journal of the American Chemical Society

2013 Volume 135, Issue 40, Page(s) 14985–14995

Abstract: ... Scheller, S.; Goenrich, M.; Thauer, R. K.; Jaun, B. J. Am. Chem. Soc. 2013, 135, DOI: 10.1021/ja406485z ...

Abstract	Ethyl-coenzyme M (CH3CH2-S-CH2CH2-SO3(-), Et-S-CoM) serves as a homologous substrate for the enzyme methyl-coenzyme M reductase (MCR) resulting in the product ethane instead of methane. The catalytic reaction proceeds via an intermediate that already contains all six C-H bonds of the product. Because product release occurs after a second, rate-limiting step, many cycles of intermediate formation and reconversion to substrate occur before a substantial amount of ethane is released. In deuterated buffer, the intermediate becomes labeled, and C-H activation in the back reaction rapidly leads to labeled Et-S-CoM, which enables intermediate formation to be detected. Here, we present a comprehensive analysis of this pre-equilibrium. (2)H- and (13)C-labeled isotopologues of Et-S-CoM were used as the substrates, and the time course of each isotopologue was followed by NMR spectroscopy. A kinetic simulation including kinetic isotope effects allowed determination of the primary and α- and β-secondary isotope effects for intermediate formation and for the C-H/C-D bond activation in the ethane-containing intermediate. The values obtained are in accordance with those found for the native substrate Me-S-CoM (see preceding publication, Scheller, S.; Goenrich, M.; Thauer, R. K.; Jaun, B. J. Am. Chem. Soc. 2013, 135, DOI: 10.1021/ja406485z) and thus imply the same catalytic mechanism for both substrates. The experiment by Floss and co-workers, demonstrating a net inversion of configuration to chiral ethane with CH3CDT-S-CoM as the substrate, is compatible with the observed rapid isotope exchange if the isotope effects measured here are taken into account.
MeSH term(s)	Ethane/metabolism ; Isotopes ; Kinetics ; Mesna/chemistry ; Mesna/metabolism ; Methanosarcina barkeri/enzymology ; Models, Molecular ; Oxidoreductases/chemistry ; Oxidoreductases/metabolism ; Protein Conformation ; Sequence Homology
Chemical Substances	Isotopes ; Oxidoreductases (EC 1.-) ; methyl coenzyme M reductase (EC 2.8.4.1) ; Ethane (L99N5N533T) ; Mesna (NR7O1405Q9)
Language	English
Publishing date	2013-10-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/ja4064876
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Article: Methyl-coenzyme M formation in methanogenic archaea. Involvement of zinc in coenzyme M activation.

Sauer, K / Thauer, R K

European journal of biochemistry

2000 Volume 267, Issue 9, Page(s) 2498–2504

Abstract: Methyl-coenzyme M (2-methylthioethane sulfonate) is the key intermediate of methane formation in methanogenic archaea. It is generated from coenzyme M (2-mercaptoethane sulfonate) in methyl transfer reactions catalyzed by proteins containing zinc. Here, ... ...

Abstract	Methyl-coenzyme M (2-methylthioethane sulfonate) is the key intermediate of methane formation in methanogenic archaea. It is generated from coenzyme M (2-mercaptoethane sulfonate) in methyl transfer reactions catalyzed by proteins containing zinc. Here, we report that, for methyltransferase MtaA from Methanosarcina barkeri, the zinc is involved in coenzyme M activation. For the experiments an inactive MtaA apoprotein was obtained by heterologous overproduction in Escherichia coli grown in the presence of 2 mM EDTA. The apoprotein was found to react with zinc or cobalt to the fully active holoenzyme. Appoximately 1 mol of transition metal was bound per mol of protein. Upon incubation of the holoenzyme with coenzyme M approximately 1 mol of proton was released per mol of zinc or cobalt. Protons were not released upon incubation of the apoprotein with coenzyme M or of the holoprotein with other thiol compounds or with methyl-coenzyme M. The findings are interpreted as indicating that the role of the transition metal in MtaA is to lower the microscopic pKa of the thiol group of coenzyme M by coordination to the zinc, and thus to increase its nucleophilicity for methyl group attack. The pKZn2+ of MtaA was re-determined and found to be > 15 and not 9.6 as previously reported by us.
MeSH term(s)	Enzyme Activation ; Mesna/analogs & derivatives ; Mesna/metabolism ; Methanosarcina barkeri/enzymology ; Methyltransferases/metabolism ; Protein Binding ; Recombinant Proteins/metabolism ; Zinc/metabolism
Chemical Substances	Recombinant Proteins ; methyl coenzyme M (53501-90-9) ; Methyltransferases (EC 2.1.1.-) ; Zinc (J41CSQ7QDS) ; Mesna (NR7O1405Q9)
Language	English
Publishing date	2000-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
DOI	10.1046/j.1432-1327.2000.01245.x
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Article: Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri.

Shima, S / Thauer, R K

Methods in enzymology

2001 Volume 331, Page(s) 317–353

MeSH term(s)	Amino Acid Sequence ; Aminohydrolases/chemistry ; Aminohydrolases/isolation & purification ; Aminohydrolases/metabolism ; Cloning, Molecular ; Coenzymes/isolation & purification ; Coenzymes/metabolism ; Escherichia coli ; Euryarchaeota/enzymology ; Euryarchaeota/growth & development ; Hydroxymethyl and Formyl Transferases/chemistry ; Hydroxymethyl and Formyl Transferases/isolation & purification ; Hydroxymethyl and Formyl Transferases/metabolism ; Methenyltetrahydrofolate Cyclohydrolase ; Molecular Sequence Data ; Oxidoreductases Acting on CH-NH Group Donors/chemistry ; Oxidoreductases Acting on CH-NH Group Donors/isolation & purification ; Oxidoreductases Acting on CH-NH Group Donors/metabolism ; Pterins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Riboflavin/analogs & derivatives ; Riboflavin/isolation & purification ; Riboflavin/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid
Chemical Substances	Coenzymes ; Pterins ; Recombinant Proteins ; coenzyme F420 (64885-97-8) ; 5,6,7,8-tetrahydromethanopterin (92481-94-2) ; Oxidoreductases Acting on CH-NH Group Donors (EC 1.5.-) ; methylenetetrahydromethanopterin dehydrogenase (EC 1.5.99.-) ; Hydroxymethyl and Formyl Transferases (EC 2.1.2.-) ; formylmethanofuran-tetrahydromethanopterin formyltransferase (EC 2.1.2.-) ; Aminohydrolases (EC 3.5.4.-) ; methenyltetrahydromethanopterin cyclohydrolase (EC 3.5.4.27) ; Methenyltetrahydrofolate Cyclohydrolase (EC 3.5.4.9) ; Riboflavin (TLM2976OFR)
Language	English
Publishing date	2001
Publishing country	United States
Document type	Comparative Study ; Journal Article
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/s0076-6879(01)31069-8
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Article: The Na(+)-translocating methyltransferase complex from methanogenic archaea.

Gottschalk, G / Thauer, R K

Biochimica et biophysica acta

2001 Volume 1505, Issue 1, Page(s) 28–36

Abstract: Methanogenic archaea are dependent on sodium ions for methane formation. A sodium ion-dependent step has been shown to be methyl transfer from N(5)-methyltetrahydromethanopterin to coenzyme M. This exergonic reaction (DeltaG degrees '=-30 kJ/mol) is ... ...

Abstract	Methanogenic archaea are dependent on sodium ions for methane formation. A sodium ion-dependent step has been shown to be methyl transfer from N(5)-methyltetrahydromethanopterin to coenzyme M. This exergonic reaction (DeltaG degrees '=-30 kJ/mol) is catalyzed by a Na(+)-translocating membrane-associated multienzyme complex composed of eight different subunits, MtrA-H. Subunit MtrA harbors a cob(I)amide prosthetic group which is methylated and demethylated in the catalytic cycle, demethylation being sodium ion-dependent. Based on the finding that in the cob(II)amide oxidation state the corrinoid is bound in a base-off/His-on configuration it is proposed that methyl transfer from MtrA to coenzyme M is associated with a conformational change of the protein and that this change drives the electrogenic translocation of the sodium ions.
MeSH term(s)	Amino Acid Sequence ; Archaeal Proteins ; Bacterial Proteins/metabolism ; Cations, Monovalent ; Cell Membrane/enzymology ; Corrinoids ; Euryarchaeota/enzymology ; Methane/metabolism ; Methyltransferases/chemistry ; Methyltransferases/metabolism ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/genetics ; Multienzyme Complexes/metabolism ; Porphyrins/chemistry ; Protein Conformation ; Sodium/metabolism
Chemical Substances	Archaeal Proteins ; Bacterial Proteins ; Cations, Monovalent ; Corrinoids ; Multienzyme Complexes ; Porphyrins ; Sodium (9NEZ333N27) ; Methyltransferases (EC 2.1.1.-) ; methylcobalamin-coenzyme M methyltransferase (EC 2.1.1.-) ; tetrahydromethanopterin S-methyltransferase (EC 2.1.1.86) ; Methane (OP0UW79H66)
Language	English
Publishing date	2001-03-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/s0005-2728(00)00274-7
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Article: Methanol:coenzyme M methyltransferase from Methanosarcina barkeri -- substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin.

Sauer, K / Thauer, R K

European journal of biochemistry

1999 Volume 261, Issue 3, Page(s) 674–681

Abstract: Methyl-coenzyme M formation from coenzyme M and methanol in Methanosarcina barkeri is catalysed by an enzyme system composed of three polypeptides MtaA, MtaB and MtaC, the latter of which harbours a corrinoid prosthetic group. We report here that MtaC ... ...

Abstract	Methyl-coenzyme M formation from coenzyme M and methanol in Methanosarcina barkeri is catalysed by an enzyme system composed of three polypeptides MtaA, MtaB and MtaC, the latter of which harbours a corrinoid prosthetic group. We report here that MtaC can be substituted by free cob(I)alamin which is methylated with methanol in an MtaB-catalysed reaction and demethylated with coenzyme M in an MtaA-catalysed reaction. Methyl transfer from methanol to coenzyme M was found to proceed at a relatively high specific activity at micromolar concentrations of cob(I)alamin. This finding was surprising because the methylation of cob(I)alamin catalysed by MtaB alone and the demethylation of methylcob(III)alamin catalysed by MtaA alone exhibit apparent Km for cob(I)alamin and methylcob(III)alamin of above 1 mm. A possible explanation is that MtaA positively affects the MtaB catalytic efficiency and vice versa by decreasing the apparent Km for their corrinoid substrates. Activation of MtaA by MtaB was methanol-dependent. In the assay for methanol:coenzyme M methyltransferase activity cob(I)alamin could be substituted by cob(I)inamide which is devoid of the nucleotide loop. Substitution was, however, only possible when the assays were supplemented with imidazole: approximately 1 mm imidazole being required for half-maximal activity. Methylation of cob(I)inamide with methanol was found to be dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction was even inhibited by imidazole. The structure and catalytic mechanism of the MtaABC complex are compared with the cobalamin-dependent methionine synthase.
MeSH term(s)	Catalysis ; Cobamides/chemistry ; Corrinoids ; Imidazoles/chemistry ; Methanosarcina barkeri/enzymology ; Methyltransferases/chemistry ; Methyltransferases/metabolism ; Porphyrins/chemistry ; Vitamin B 12/chemistry
Chemical Substances	Cobamides ; Corrinoids ; Imidazoles ; Porphyrins ; cobinamide (13497-85-3) ; Methyltransferases (EC 2.1.1.-) ; methanol-2-mercaptoethanesulfonic acid methyltransferase (EC 2.1.1.-) ; Vitamin B 12 (P6YC3EG204)
Language	English
Publishing date	1999-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3032-6
ISSN	1432-1033 ; 0014-2956
ISSN (online)	1432-1033
ISSN	0014-2956
DOI	10.1046/j.1432-1327.1999.00355.x
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Book ; Online: Rohstoffe für die Energieversorgung der Zukunft

Angerer, G. / Buchholz, P. / Gutzmer, J. / Hagelüken, C. / Herzig, Peter / Littke, R. / Thauer, R. K. / Wellmer, F.-W.

Geologie - Märkte - Umwelteinflüsse

2016

Language	English
Publisher	acatech - Deutsche Akademie der Technikwissenschaften
Publishing country	de
Document type	Book ; Online
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Article ; Online: Hydrogen formation and its regulation in Ruminococcus albus: involvement of an electron-bifurcating [FeFe]-hydrogenase, of a non-electron-bifurcating [FeFe]-hydrogenase, and of a putative hydrogen-sensing [FeFe]-hydrogenase.

Zheng, Yanning / Kahnt, Jörg / Kwon, In Hyuk / Mackie, Roderick I / Thauer, Rudolf K

Journal of bacteriology

2014 Volume 196, Issue 22, Page(s) 3840–3852

Abstract: ... we report that R. albus 7 grown in batch culture on glucose contained, besides a ferredoxin-dependent [FeFe ... are required only when R. albus grows at high H2 partial pressures, HydS could be a H2-sensing [FeFe ...

Abstract	Ruminococcus albus 7 has played a key role in the development of the concept of interspecies hydrogen transfer. The rumen bacterium ferments glucose to 1.3 acetate, 0.7 ethanol, 2 CO2, and 2.6 H2 when growing in batch culture and to 2 acetate, 2 CO2, and 4 H2 when growing in continuous culture in syntrophic association with H2-consuming microorganisms that keep the H2 partial pressure low. The organism uses NAD(+) and ferredoxin for glucose oxidation to acetyl coenzyme A (acetyl-CoA) and CO2, NADH for the reduction of acetyl-CoA to ethanol, and NADH and reduced ferredoxin for the reduction of protons to H2. Of all the enzymes involved, only the enzyme catalyzing the formation of H2 from NADH remained unknown. Here, we report that R. albus 7 grown in batch culture on glucose contained, besides a ferredoxin-dependent [FeFe]-hydrogenase (HydA2), a ferredoxin- and NAD-dependent electron-bifurcating [FeFe]-hydrogenase (HydABC) that couples the endergonic formation of H2 from NADH to the exergonic formation of H2 from reduced ferredoxin. Interestingly, hydA2 is adjacent to the hydS gene, which is predicted to encode an [FeFe]-hydrogenase with a C-terminal PAS domain. We showed that hydS and hydA2 are part of a larger transcriptional unit also harboring putative genes for a bifunctional acetaldehyde/ethanol dehydrogenase (Aad), serine/threonine protein kinase, serine/threonine protein phosphatase, and a redox-sensing transcriptional repressor. Since HydA2 and Aad are required only when R. albus grows at high H2 partial pressures, HydS could be a H2-sensing [FeFe]-hydrogenase involved in the regulation of their biosynthesis.
MeSH term(s)	Acetyl Coenzyme A/metabolism ; Aldehyde Oxidoreductases/genetics ; Aldehyde Oxidoreductases/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Electron Transport ; Fermentation ; Formate Dehydrogenases/genetics ; Formate Dehydrogenases/metabolism ; Gene Expression Regulation, Bacterial/physiology ; Gene Expression Regulation, Enzymologic/physiology ; Glucose/metabolism ; Hydrogen/metabolism ; Hydrogenase/metabolism ; Iron/metabolism ; NAD ; NADP/metabolism ; Pyruvate Synthase/genetics ; Pyruvate Synthase/metabolism ; Ruminococcus/metabolism
Chemical Substances	Bacterial Proteins ; NAD (0U46U6E8UK) ; NADP (53-59-8) ; Acetyl Coenzyme A (72-89-9) ; Hydrogen (7YNJ3PO35Z) ; Iron (E1UOL152H7) ; Hydrogenase (EC 1.12.7.2) ; Formate Dehydrogenases (EC 1.17.1.9) ; Aldehyde Oxidoreductases (EC 1.2.-) ; Pyruvate Synthase (EC 1.2.7.1) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2014-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.02070-14
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