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Diversifying Metal–Ligand Cooperative Catalysis in Semi‐Synthetic [Mn]‐Hydrogenases.
- Published in:
- Angewandte Chemie, 2021, v. 133, n. 24, p. 13462, doi. 10.1002/ange.202100443
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- Article
X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases.
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- Angewandte Chemie, 2019, v. 131, n. 51, p. 18883, doi. 10.1002/ange.201908258
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- Article
The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates.
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- Angewandte Chemie, 2019, v. 131, n. 11, p. 3544, doi. 10.1002/ange.201813465
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- Article
How [Fe]‐Hydrogenase from Methanothermobacter is Protected Against Light and Oxidative Stress.
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- Angewandte Chemie, 2018, v. 130, n. 46, p. 15276, doi. 10.1002/ange.201807203
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Dioxygen Sensitivity of [Fe]‐Hydrogenase in the Presence of Reducing Substrates.
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- Angewandte Chemie, 2018, v. 130, n. 18, p. 5011, doi. 10.1002/ange.201712293
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- Article
A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC.
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- Angewandte Chemie, 2017, v. 129, n. 36, p. 10946, doi. 10.1002/ange.201705605
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- Article
Biologische Methanbildung: Bestätigung des Reaktionsmechanismus durch spektroskopische Charakterisierung eines Schlüsselintermediats.
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- Angewandte Chemie, 2016, v. 128, n. 44, p. 13848, doi. 10.1002/ange.201606269
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- Article
Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation.
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- Angewandte Chemie, 2016, v. 128, n. 36, p. 10788, doi. 10.1002/ange.201603882
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- Article
Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis.
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- Angewandte Chemie, 2016, v. 128, n. 33, p. 9800, doi. 10.1002/ange.201604352
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- Article
How [Fe]‐Hydrogenase from Methanothermobacter is Protected Against Light and Oxidative Stress.
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- Angewandte Chemie International Edition, 2018, v. 57, n. 46, p. 15056, doi. 10.1002/anie.201807203
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- Publication type:
- Article
Dioxygen Sensitivity of [Fe]-Hydrogenase in the Presence of Reducing Substrates.
- Published in:
- Angewandte Chemie International Edition, 2018, v. 57, n. 18, p. 4917, doi. 10.1002/anie.201712293
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- Publication type:
- Article
A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC.
- Published in:
- Angewandte Chemie International Edition, 2017, v. 56, n. 36, p. 10806, doi. 10.1002/anie.201705605
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- Article
The Biological Methane-Forming Reaction: Mechanism Confirmed Through Spectroscopic Characterization of a Key Intermediate.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 44, p. 13648, doi. 10.1002/anie.201606269
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- Article
Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 36, p. 10630, doi. 10.1002/anie.201603882
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- Publication type:
- Article
Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 33, p. 9648, doi. 10.1002/anie.201604352
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- Article
Inside Back Cover: Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis (Angew. Chem. Int. Ed. 48/2013).
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- Angewandte Chemie International Edition, 2013, v. 52, n. 48, p. 12745, doi. 10.1002/anie.201308951
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- Article
Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis.
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- Angewandte Chemie International Edition, 2013, v. 52, n. 48, p. 12555, doi. 10.1002/anie.201306745
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- Article
Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H<sub>2</sub>-Activation Site.
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- Angewandte Chemie International Edition, 2013, v. 52, n. 37, p. 9656, doi. 10.1002/anie.201305089
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- Article
Structures of F<sub>420</sub>H<sub>2</sub>:NADP<sup>+</sup> oxidoreductase with and without its substrates bound.
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- EMBO Journal, 2001, v. 20, n. 23, p. 6561, doi. 10.1093/emboj/20.23.6561
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- Article
Methane as Fuel for Anaerobic Microorganisms.
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- Annals of the New York Academy of Sciences, 2008, v. 1125, p. 158, doi. 10.1196/annals.1419.000
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- Article
Innenrücktitelbild: Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis (Angew. Chem. 48/2013).
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- Angewandte Chemie, 2013, v. 125, n. 48, p. 12979, doi. 10.1002/ange.201308951
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- Article
Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis.
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- Angewandte Chemie, 2013, v. 125, n. 48, p. 12787, doi. 10.1002/ange.201306745
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- Publication type:
- Article
Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H<sub>2</sub>-Activation Site.
- Published in:
- Angewandte Chemie, 2013, v. 125, n. 37, p. 9838, doi. 10.1002/ange.201305089
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- Article
Iron-Chromophore Circular Dichroism of [Fe]-Hydrogenase: The Conformational Change Required for H<sub>2</sub> Activation.
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- Angewandte Chemie, 2010, v. 122, n. 51, p. 10113, doi. 10.1002/ange.201006255
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- Article
MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode.
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- Scientific Reports, 2016, p. 28226, doi. 10.1038/srep28226
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- Article
A third type of hydrogenase catalyzing H<sub>2</sub> activation.
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- Chemical Record, 2007, v. 7, n. 1, p. 37, doi. 10.1002/tcr.20111
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- Article
Isolation of an H<sub>2</sub>‐dependent electron‐bifurcating CO<sub>2</sub>‐reducing megacomplex with MvhB polyferredoxin from Methanothermobacter marburgensis.
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- FEBS Journal, 2024, v. 291, n. 11, p. 2449, doi. 10.1111/febs.17115
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- Article
[Fe]‐Hydrogenase, Cofactor Biosynthesis and Engineering.
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- ChemBioChem, 2023, v. 24, n. 20, p. 1, doi. 10.1002/cbic.202300330
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- Article
Cu<sup>I</sup> and H<sub>2</sub>O<sub>2</sub> Inactivate and Fe<sup>II</sup> Inhibits [Fe]-Hydrogenase at Very Low Concentrations.
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- ChemBioChem, 2015, v. 16, n. 13, p. 1861, doi. 10.1002/cbic.201500318
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- Article
Biogeochemistry: Methane and microbes.
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- Nature, 2006, v. 440, n. 7086, p. 878, doi. 10.1038/440878a
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- Article
Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri.
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- Proteins, 1996, v. 26, n. 1, p. 118, doi. 10.1002/(SICI)1097-0134(199609)26:1<118::AID-PROT12>3.0.CO;2-J
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Towards a functional identification of catalytically inactive [Fe]-hydrogenase paralogs.
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- FEBS Journal, 2015, v. 282, n. 17, p. 3412, doi. 10.1111/febs.13351
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- Article
Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea.
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- FEBS Journal, 2007, v. 274, n. 18, p. 4913, doi. 10.1111/j.1742-4658.2007.06016.x
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- Article
Structure of coenzyme F<sub>420</sub>H<sub>2</sub> oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O<sub>2</sub> to H<sub>2</sub>O.
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- FEBS Journal, 2007, v. 274, n. 6, p. 1588, doi. 10.1111/j.1742-4658.2007.05706.x
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- Article
Cover Feature: Unveiling the Binding Modes of the Crystallophore, a Terbium‐based Nucleating and Phasing Molecular Agent for Protein Crystallography (Chem. Eur. J. 39/2018).
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- Chemistry - A European Journal, 2018, v. 24, n. 39, p. 9701, doi. 10.1002/chem.201802734
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- Article
Unveiling the Binding Modes of the Crystallophore, a Terbium‐based Nucleating and Phasing Molecular Agent for Protein Crystallography.
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- Chemistry - A European Journal, 2018, v. 24, n. 39, p. 9739, doi. 10.1002/chem.201802172
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- Article
Acyl and CO Ligands in the [Fe]‐Hydrogenase Cofactor Scramble upon Photolysis.
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- Angewandte Chemie, 2024, v. 136, n. 6, p. 1, doi. 10.1002/ange.202316478
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- Article
The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the [Fe]‐Hydrogenase Cofactor.
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- Angewandte Chemie, 2022, v. 134, n. 50, p. 1, doi. 10.1002/ange.202213239
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- Article
In Vitro Biosynthesis of the [Fe]‐Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors.
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- Angewandte Chemie, 2022, v. 134, n. 22, p. 1, doi. 10.1002/ange.202200994
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- Article
A reversed genetic approach reveals the coenzyme specificity and other catalytic properties of three enzymes putatively involved in anaerobic oxidation of methane with sulfate.
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- Environmental Microbiology, 2014, v. 16, n. 11, p. 3431, doi. 10.1111/1462-2920.12475
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- Article
Immunological detection of enzymes for sulfate reduction in anaerobic methane-oxidizing consortia.
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- Environmental Microbiology, 2013, v. 15, n. 5, p. 1561, doi. 10.1111/1462-2920.12003
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- Article
Bacterial enzymes for dissimilatory sulfate reduction in a marine microbial mat (Black Sea) mediating anaerobic oxidation of methane.
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- Environmental Microbiology, 2011, v. 13, n. 5, p. 1370, doi. 10.1111/j.1462-2920.2011.02443.x
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- Article
Denitrifying bacteria anaerobically oxidize methane in the absence of Archaea.
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- Environmental Microbiology, 2008, v. 10, n. 11, p. 3164, doi. 10.1111/j.1462-2920.2008.01724.x
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- Article
Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor.
- Published in:
- Nature Communications, 2015, v. 6, n. 4, p. 6895, doi. 10.1038/ncomms7895
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- Article
Identification of trf2 mutants of Drosophila with defects in anterior spiracle eversion.
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- Archives of Insect Biochemistry & Physiology, 2007, v. 64, n. 4, p. 157, doi. 10.1002/arch.20166
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- Article
Acyl and CO Ligands in the [Fe]‐Hydrogenase Cofactor Scramble upon Photolysis.
- Published in:
- Angewandte Chemie International Edition, 2024, v. 63, n. 6, p. 1, doi. 10.1002/anie.202316478
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- Publication type:
- Article
The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the [Fe]‐Hydrogenase Cofactor.
- Published in:
- Angewandte Chemie International Edition, 2022, v. 61, n. 50, p. 1, doi. 10.1002/anie.202213239
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- Publication type:
- Article
In Vitro Biosynthesis of the [Fe]‐Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors.
- Published in:
- Angewandte Chemie International Edition, 2022, v. 61, n. 22, p. 1, doi. 10.1002/anie.202200994
- By:
- Publication type:
- Article
Diversifying Metal–Ligand Cooperative Catalysis in Semi‐Synthetic [Mn]‐Hydrogenases.
- Published in:
- Angewandte Chemie International Edition, 2021, v. 60, n. 24, p. 13350, doi. 10.1002/anie.202100443
- By:
- Publication type:
- Article
X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases.
- Published in:
- Angewandte Chemie International Edition, 2019, v. 58, n. 51, p. 18710, doi. 10.1002/anie.201908258
- By:
- Publication type:
- Article