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Methyl-Coenzyme M Reductase from Methanogenic Archaea: Isotope Effects on Label Exchange and Ethane Formation with the Homologous Substrate Ethyl-Coenzyme M

Journal of the American Chemical Society, 2013-10, Vol.135 (40), p.14985-14995

2013

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Methyl-Coenzyme M Reductase from Methanogenic Archaea: Isotope Effects on the Formation and Anaerobic Oxidation of Methane

Journal of the American Chemical Society, 2013-10, Vol.135 (40), p.14975-14984

2013

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An ancient pathway combining carbon dioxide fixation with the generation and utilization of a sodium ion gradient for ATP synthesis

PloS one, 2012-03, Vol.7 (3), p.e33439-e33439

2012

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More Than 200 Genes Required for Methane Formation from H2 and CO2 and Energy Conservation Are Present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus

Archaea (Vancouver), 2011-01, Vol.2011 (2011), p.1-23

2011

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More Than 200 Genes Required for Methane Formation from H_2 and CO_2 and Energy Conservation Are Present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus

Archaea, 2011, Vol.2011, p.113-135

2011

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Complete Genome Sequence of Methanothermobacter marburgensis, a Methanoarchaeon Model Organism

Journal of Bacteriology, 2010-11, Vol.192 (21), p.5850-5851

2010

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Zwischenprodukte im Katalysezyklus von Methyl‐Coenzym‐M‐ Reduktase: Das Muster des Isotopenaustauschs ist in Einklang mit der Bildung eines σ‐Alkan‐Nickel‐Komplexes

Angewandte Chemie, 2010-10, Vol.122 (44), p.8289-8292

2010

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Zwischenprodukte im Katalysezyklus von Methyl-Coenzym-M- Reduktase: Das Muster des Isotopenaustauschs ist in Einklang mit der Bildung eines σ-Alkan-Nickel-Komplexes

Angewandte Chemie, 2010-10, Vol.122 (44), p.8289-8292

2010

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Zwischenprodukte im Katalysezyklus von Methyl-Coenzym-M- Reduktase: Das Muster des Isotopenaustauschs ist in Einklang mit der Bildung eines [sigma]-Alkan-Nickel-Komplexes

Angewandte Chemie, 2010-10, Vol.122 (44), p.8289

2010

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Intermediates in the Catalytic Cycle of Methyl Coenzyme M Reductase: Isotope Exchange is Consistent with Formation of a σ‐Alkane-Nickel Complex

Angewandte Chemie (International ed.), 2010-10, Vol.49 (44), p.8112-8115

2010

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Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H 2 Storage

Annual review of biochemistry, 2010, Vol.79 (1), p.507-536

2010

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The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane

Nature, 2010-06, Vol.465 (7298), p.606-608

2010

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Binding of Coenzyme B Induces a Major Conformational Change in the Active Site of Methyl-Coenzyme M Reductase

Journal of the American Chemical Society, 2010-01, Vol.132 (2), p.567-575

2010

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Hydrogenases from methanogenic archaea, nickel, a novel cofactor, and H2 storage

Annual review of biochemistry, 2010, Vol.79, p.507-507

2010

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Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase

Journal of biological inorganic chemistry, 2008-11, Vol.13 (8), p.1275-1289

2008

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A Nickel Hydride Complex in the Active Site of Methyl-Coenzyme M Reductase: Implications for the Catalytic Cycle

Journal of the American Chemical Society, 2008-08, Vol.130 (33), p.10907-10920

2008

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Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy

Journal of biological inorganic chemistry, 2007-11, Vol.12 (8), p.1097-1105

2007

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A Nickel-Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation

Angewandte Chemie, 2006-05, Vol.118 (22), p.3684-3689

2006

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A Nickel-Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation

Angewandte Chemie (International ed.), 2006-05, Vol.45 (22), p.3602-3607

2006

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A Nickel–Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation

Angewandte Chemie, 2006-05, Vol.118 (22), p.3684-3689

2006

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Spin Density and Coenzyme M Coordination Geometry of the ox1 Form of Methyl-Coenzyme M Reductase: A Pulse EPR Study

Journal of the American Chemical Society, 2005-12, Vol.127 (50), p.17744-17755

2005

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Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis

Archives of microbiology, 2005-10, Vol.184 (1), p.41-48

2005

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Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B

Journal of biological inorganic chemistry, 2005-06, Vol.10 (4), p.333-342

2005

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How an Enzyme Binds the C1 Carrier Tetrahydromethanopterin

The Journal of biological chemistry, 2005-04, Vol.280 (14), p.13712-13719

2005

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How an Enzyme Binds the C sub(1) Carrier Tetrahydromethanopterin: Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1

The Journal of biological chemistry, 2005-04, Vol.280 (14), p.13712-13719

2005

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Methyl-Coenzyme M Reductase from Methanogenic Archaea: Isotope Effects on Label Exchange and Ethane Formation with the Homologous Substrate Ethyl-Coenzyme M

Methyl-Coenzyme M Reductase from Methanogenic Archaea: Isotope Effects on the Formation and Anaerobic Oxidation of Methane

An ancient pathway combining carbon dioxide fixation with the generation and utilization of a sodium ion gradient for ATP synthesis

More Than 200 Genes Required for Methane Formation from H2 and CO2 and Energy Conservation Are Present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus

More Than 200 Genes Required for Methane Formation from H_2 and CO_2 and Energy Conservation Are Present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus

Complete Genome Sequence of Methanothermobacter marburgensis, a Methanoarchaeon Model Organism

Zwischenprodukte im Katalysezyklus von Methyl‐Coenzym‐M‐ Reduktase: Das Muster des Isotopenaustauschs ist in Einklang mit der Bildung eines σ‐Alkan‐Nickel‐Komplexes

Zwischenprodukte im Katalysezyklus von Methyl-Coenzym-M- Reduktase: Das Muster des Isotopenaustauschs ist in Einklang mit der Bildung eines σ-Alkan-Nickel-Komplexes

Zwischenprodukte im Katalysezyklus von Methyl-Coenzym-M- Reduktase: Das Muster des Isotopenaustauschs ist in Einklang mit der Bildung eines [sigma]-Alkan-Nickel-Komplexes

Intermediates in the Catalytic Cycle of Methyl Coenzyme M Reductase: Isotope Exchange is Consistent with Formation of a σ‐Alkane-Nickel Complex

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H 2 Storage

The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane

Binding of Coenzyme B Induces a Major Conformational Change in the Active Site of Methyl-Coenzyme M Reductase

Hydrogenases from methanogenic archaea, nickel, a novel cofactor, and H2 storage

Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase

A Nickel Hydride Complex in the Active Site of Methyl-Coenzyme M Reductase: Implications for the Catalytic Cycle

Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy

A Nickel-Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation

A Nickel-Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation

A Nickel–Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation

Spin Density and Coenzyme M Coordination Geometry of the ox1 Form of Methyl-Coenzyme M Reductase: A Pulse EPR Study

Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis

Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B

How an Enzyme Binds the C1 Carrier Tetrahydromethanopterin

How an Enzyme Binds the C sub(1) Carrier Tetrahydromethanopterin: Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1

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