Works by Shima, Seigo
Results: 76
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
Diversifying Metal–Ligand Cooperative Catalysis in Semi‐Synthetic [Mn]‐Hydrogenases.
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- 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
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
[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
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
Iron-Chromophore Circular Dichroism of [Fe]-Hydrogenase: The Conformational Change Required for H<sub>2</sub> Activation.
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- Angewandte Chemie International Edition, 2010, v. 49, n. 51, p. 9917, doi. 10.1002/anie.201006255
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- Article
The Crystal Structure of an [Fe]-Hydrogenase-Substrate Complex Reveals the Framework for H<sub>2</sub> Activation.
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- Angewandte Chemie International Edition, 2009, v. 48, n. 35, p. 6457, doi. 10.1002/anie.200902695
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- Article
Crystal structure of archaeal HMG‐CoA reductase: insights into structural changes of the C‐terminal helix of the class‐I enzyme.
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- FEBS Letters, 2019, v. 593, n. 5, p. 543, doi. 10.1002/1873-3468.13331
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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
The exchange activities of [Fe] hydrogenase (iron–sulfur-cluster-free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases.
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- Journal of Biological Inorganic Chemistry (JBIC), 2008, v. 13, n. 1, p. 97, doi. 10.1007/s00775-007-0302-2
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- Article
Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically.
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- Nature, 2012, v. 481, n. 7379, p. 98, doi. 10.1038/nature10663
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- Article
Crystal Structures of [Fe]-Hydrogenase from Methanolacinia paynteri Suggest a Path of the FeGP-Cofactor Incorporation Process.
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- Inorganics, 2020, v. 8, n. 9, p. 50, doi. 10.3390/inorganics8090050
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- Article
Dentatorubral-pallidoluysian atrophy protein is phosphorylated by c-Jun NH2-terminal kinase.
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- Human Molecular Genetics, 2003, v. 12, n. 13, p. 1535, doi. 10.1093/hmg/ddg168
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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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- Article
Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor.
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- Nature Communications, 2015, v. 6, n. 4, p. 6895, doi. 10.1038/ncomms7895
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- Article
Protein crystal structure determination with the crystallophore, a nucleating and phasing agent.
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- Journal of Applied Crystallography, 2019, v. 52, n. 4, p. 722, doi. 10.1107/S1600576719006381
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- Article
Nickel-Iron-Selenium Hydrogenases - An Overview Structure and Function of [Fe]-Hydrogenase and its Iron-Guanylylpyridinol (FeGP) Cofactor Magnetic Properties of [FeFe]-Hydrogenases: A Theoretical Investigation Based on Extended QM and QM/MM Models of the H-Cluster and Its Surroundings Solar Hydrogen Evolution with Hydrogenases: From Natural to Hybrid Systems Molecular Electrocatalysts for the Oxidation of Hydrogen and the Production of Hydrogen - The Role of Pendant Amines as Proton Relays (Eur. J. Inorg. Chem. 7/2011)
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- European Journal of Inorganic Chemistry, 2011, v. 2011, n. 7, p. n/a, doi. 10.1002/ejic.201190015
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- Article
Structure and Function of [Fe]-Hydrogenase and its Iron-Guanylylpyridinol (FeGP) Cofactor.
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- European Journal of Inorganic Chemistry, 2011, v. 2011, n. 7, p. 963, doi. 10.1002/ejic.201000955
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- Article
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
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
- By:
- 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
The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates.
- Published in:
- Angewandte Chemie International Edition, 2019, v. 58, n. 11, p. 3506, doi. 10.1002/anie.201813465
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- Publication type:
- 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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- Article
A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]‐hydrogenase cofactor biosynthesis.
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- FEBS Letters, 2014, v. 588, n. 17, p. 2789, doi. 10.1016/j.febslet.2014.05.059
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- Article
Isocyanides inhibit [Fe]-hydrogenase with very high affinity
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- FEBS Letters, 2011, v. 585, n. 2, p. 353, doi. 10.1016/j.febslet.2010.12.014
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- Article
The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex
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- FEBS Letters, 2009, v. 583, n. 3, p. 585, doi. 10.1016/j.febslet.2009.01.017
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- Article
F<sub>420</sub>H<sub>2</sub> oxidase (FprA) fromMethanobrevibacter arboriphilus, a coenzyme F<sub>420</sub>-dependent enzyme involved in O<sub>2</sub> detoxification.
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- Archives of Microbiology, 2004, v. 182, n. 2/3, p. 126, doi. 10.1007/s00203-004-0675-3
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- Article
Protection of Methanosarcina barkeri against oxidative stress: identification and characterization of an iron superoxide dismutase.
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- Archives of Microbiology, 2000, v. 174, n. 3, p. 213, doi. 10.1007/s002030000180
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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 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
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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- 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
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
Iron-Chromophore Circular Dichroism of [Fe]-Hydrogenase: The Conformational Change Required for H<sub>2</sub> Activation.
- Published in:
- Angewandte Chemie, 2010, v. 122, n. 51, p. 10113, doi. 10.1002/ange.201006255
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- Article
The Cofactor of the IronSulfur Cluster Free Hydrogenase Hmd: Structure of the Light-Inactivation Product ( The authors thank Prof. Dr. Stefan Berger (Universität Leipzig) for the determination of the high-resolution mass data, Dr. Stefan Bartoschek and Dr. Peter Grice (University of Cambridge, UK) for recording the broadband <sup>13</sup>C NMR spectrum on a <sup>13</sup>C detection cryoprobe, Prof. Dr. Thomas Carell (Universität Marburg) for helpful discussions, and Dr. Antonio Pierik for assistance with the fluorescence measurements. L.V. was funded by the European research network HPRN CT 2000 00092. )
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- Angewandte Chemie, 2004, v. 116, n. 19, p. 2601, doi. 10.1002/ange.200353763
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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
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
How [Fe]‐Hydrogenase from Methanothermobacter is Protected Against Light and Oxidative Stress.
- Published in:
- Angewandte Chemie, 2018, v. 130, n. 46, p. 15276, doi. 10.1002/ange.201807203
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- Publication type:
- Article
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