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Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction

Science (American Association for the Advancement of Science), 2017-08, Vol.357 (6352), p.699-703

2017

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Methanothermobacter — Biokatalysator für die Energiewende

Biospektrum, 2021-02, Vol.27 (1), p.14-17

2021

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A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor

Nature chemistry, 2019-07, Vol.11 (7), p.669

2019

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Three-megadalton complex of methanogenic electron-bifurcating and CO2-fixing enzymes

Science (American Association for the Advancement of Science), 2021-09, Vol.373 (6559), p.1151-1156

2021

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Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation

Angewandte Chemie (International ed.), 2016-08, Vol.55 (36), p.10630-10633

2016

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Mode of action uncovered for the specific reduction of methane emissions from ruminants by the small molecule 3-nitrooxypropanol

Proceedings of the National Academy of Sciences - PNAS, 2016-05, Vol.113 (22), p.6172-6177

2016

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Krypton-derivatization highlights O2-channeling in a four-electron reducing oxidase

Chemical communications (Cambridge, England), 2020-09, Vol.56 (74), p.10863-10866

2020

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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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Structure and Function of [Fe]-Hydrogenase and its Iron-Guanylylpyridinol (FeGP) Cofactor

European Journal of Inorganic Chemistry, 2011-03, Vol.2011 (7), p.963-972

2011

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X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases

Angewandte Chemie (International ed.), 2019-12, Vol.58 (51), p.18710-18714

International ed. in English, 2019

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Phylogenetic and Structural Comparisons of the Three Types of Methyl Coenzyme M Reductase from Methanococcales and Methanobacteriales

Journal of bacteriology, 2017-08, Vol.199 (16)

2017

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Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site

Science (American Association for the Advancement of Science), 2008-07, Vol.321 (5888), p.572-575

2008

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A third type of hydrogenase catalyzing H2 activation

Chemical record, 2007, Vol.7 (1), p.37-46

2007

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Crystal Structure of an [Fe]-Hydrogenase-Substrate Complex Reveals the Framework for H₂ Activation

Angewandte Chemie (International ed.), 2009-01, Vol.48 (35), p.6457-6460

2009

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Reconstitution of [Fe]-hydrogenase using model complexes

Nature chemistry, 2015-12, Vol.7 (12), p.995

2015

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De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy

eLife, 2013-03, Vol.2

2013

Volltextzugriff (PDF)

MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode

Scientific reports, 2016-06, Vol.6 (1), p.28226-28226, Article 28226

2016

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Denitrifying bacteria anaerobically oxidize methane in the absence of Archaea

Environmental microbiology, 2008-11, Vol.10 (11), p.3164-3173

2008

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A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis

FEBS letters, 2014-08, Vol.588 (17), p.2789-2793

2014

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The F₄₂₀-reducing [NiFe]-hydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member

Journal of molecular biology, 2014-07, Vol.426 (15), p.2813-2826

2014

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Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor

Nature communications, 2015-04, Vol.6 (1), p.6895-6895, Article 6895

2015

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The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex

FEBS letters, 2009-02, Vol.583 (3), p.585-590

2009

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Methyl-coenzyme M reductase and the anaerobic oxidation of methane in methanotrophic Archaea

Current opinion in microbiology, 2005-12, Vol.8 (6), p.643-648

2005

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Biosynthesis of the Iron-Guanylylpyridinol Cofactor of [Fe]-Hydrogenase in Methanogenic Archaea as Elucidated by Stable-Isotope Labeling

Journal of the American Chemical Society, 2012-02, Vol.134 (6), p.3271-3280

2012

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The Biological Methane-Forming Reaction: Mechanism Confirmed Through Spectroscopic Characterization of a Key Intermediate

Angewandte Chemie (International ed.), 2016-10, Vol.55 (44), p.13648-13649

Shima, Seigo

International ed. in English, 2016

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Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction

Methanothermobacter — Biokatalysator für die Energiewende

A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor

Three-megadalton complex of methanogenic electron-bifurcating and CO2-fixing enzymes

Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation

Mode of action uncovered for the specific reduction of methane emissions from ruminants by the small molecule 3-nitrooxypropanol

Krypton-derivatization highlights O2-channeling in a four-electron reducing oxidase

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

Structure and Function of [Fe]-Hydrogenase and its Iron-Guanylylpyridinol (FeGP) Cofactor

X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases

Phylogenetic and Structural Comparisons of the Three Types of Methyl Coenzyme M Reductase from Methanococcales and Methanobacteriales

Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site

A third type of hydrogenase catalyzing H2 activation

Crystal Structure of an [Fe]-Hydrogenase-Substrate Complex Reveals the Framework for H₂ Activation

Reconstitution of [Fe]-hydrogenase using model complexes

De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy

MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode

Denitrifying bacteria anaerobically oxidize methane in the absence of Archaea

A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis

The F₄₂₀-reducing [NiFe]-hydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member

Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor

The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex

Methyl-coenzyme M reductase and the anaerobic oxidation of methane in methanotrophic Archaea

Biosynthesis of the Iron-Guanylylpyridinol Cofactor of [Fe]-Hydrogenase in Methanogenic Archaea as Elucidated by Stable-Isotope Labeling

The Biological Methane-Forming Reaction: Mechanism Confirmed Through Spectroscopic Characterization of a Key Intermediate

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