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Chemistry

D-Index
57
Citations
11363
World Ranking
11106
National Ranking
806

Overview

Seigo Shima is affiliated with the Max Planck Society in Germany, focusing on research in energy, biochemistry, genetics, molecular biology, and chemistry. Their work concentrates particularly on renewable energy, sustainability, materials chemistry, inorganic chemistry, molecular biology, and biochemistry.

The scientist's research engages with several main topics, including:

  • Metalloenzymes and iron-sulfur proteins
  • Electrocatalysts for energy conversion
  • Metal-catalyzed oxygenation mechanisms
  • Hydrogen storage and materials
  • Amino acid enzymes and metabolism
  • Enzyme structure and function
  • Crystallization and solubility studies

Seigo Shima has contributed to different publication venues, with multiple works appearing in:

  • Angewandte Chemie International Edition
  • Angewandte Chemie
  • The Cambridge Structural Database
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Catalysis

Recent publications by Seigo Shima include:

  • "Three-megadalton complex of methanogenic electron-bifurcating and CO 2 -fixing enzymes," 2021, Science
  • "Methanogenesis involves direct hydride transfer from H2 to an organic substrate," 2020, Nature Reviews Chemistry
  • "Structural Basis of Hydrogenotrophic Methanogenesis," 2020, Annual Review of Microbiology
  • "Methane monooxygenases; physiology, biochemistry and structure," 2023, Catalysis Science & Technology
  • "Diversifying Metal-Ligand Cooperative Catalysis in Semi-Synthetic [Mn]-Hydrogenases," 2021, Angewandte Chemie International Edition

The scientist frequently collaborates with other researchers. Notable co-authors include:

  • Tristan Wagner
  • Gangfeng Huang
  • Jörg Kahnt
  • Manuel Gehl
  • Francisco J. Arriaza-Gallardo

Best Publications

  • Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.

    Ulrich Ermler;Wolfgang Grabarse;Seigo Shima;Marcel Goubeaud

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

    Seigo Shima;Oliver Pilak;Sonja Vogt;Michael Schick

  • Denitrifying bacteria anaerobically oxidize methane in the absence of Archaea.

    Katharina F. Ettwig;Seigo Shima;Katinka T. Van De Pas-Schoonen;Jörg Kahnt

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

    Rudolf K. Thauer;Anne-Kristin Kaster;Meike Goenrich;Michael Schick

  • A conspicuous nickel protein in microbial mats that oxidize methane anaerobically

    Martin Krüger;Anke Meyerdierks;Frank Oliver Glöckner;Rudolf Amann

  • A third type of hydrogenase catalyzing H2 activation.

    Seigo Shima;Rudolf K. Thauer

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

    Evert C. Duin;Tristan Wagner;Seigo Shima;Divya Prakash

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

    Takeshi Hiromoto;Kenichi Ataka;Oliver Pilak;Sonja Vogt

  • Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy.

    Erica J Lyon;Seigo Shima;Reinhard Boecher;Rudolf K Thauer

  • Methane as fuel for anaerobic microorganisms.

    Rudolf K. Thauer;Seigo Shima

  • UV-A/blue-light inactivation of the 'metal-free' hydrogenase (Hmd) from methanogenic archaea The enzyme contains functional iron after all

    Erica J. Lyon;Seigo Shima;Gerrit Buurman;Shantanu Chowdhuri

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

    Tristan Wagner;Jürgen Koch;Ulrich Ermler;Seigo Shima

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

    Seigo Shima;Rudolf K Thauer

  • Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation

    Wolfgang Grabarse;Felix Mahlert;Seigo Shima;Rudolf K Thauer

  • On the Mechanism of Biological Methane Formation: Structural Evidence for Conformational Changes in Methyl-Coenzyme M Reductase Upon Substrate Binding

    Wolfgang Grabarse;Felix Mahlert;Evert C. Duin;Marcel Goubeaud

  • Mössbauer Studies of the Iron−Sulfur Cluster-Free Hydrogenase: The Electronic State of the Mononuclear Fe Active Site

    Seigo Shima;Erica J. Lyon;Rudolf K. Thauer;Bernd Mienert

  • The Cofactor of the Iron–Sulfur Cluster Free Hydrogenase Hmd: Structure of the Light-Inactivation Product

    Seigo Shima;Erica J. Lyon;Melanie Sordel-Klippert;Manuela Kauss

  • Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically

    Seigo Shima;Martin Krueger;Tobias Weinert;Ulrike Demmer

  • The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters

    Tristan Wagner;Ulrich Ermler;Seigo Shima;Seigo Shima

  • The crystal structure of an [Fe]-hydrogenase-substrate complex reveals the framework for H2 activation.

    Takeshi Hiromoto;Eberhard Warkentin;Johanna Moll;Ulrich Ermler

  • Active sites of transition-metal enzymes with a focus on nickel.

    Ulrich Ermler;Wolfgang Grabarse;Seigo Shima;Marcel Goubeaud

  • The Iron-Sulfur Cluster-free Hydrogenase (Hmd) Is a Metalloenzyme with a Novel Iron Binding Motif

    Malgorzata Korbas;Sonja Vogt;Wolfram Meyer-Klaucke;Eckhard Bill

Frequent Co-Authors

Ulrich Ermler
Ulrich Ermler Max Planck Society
Rudolf K. Thauer
Rudolf K. Thauer Max Planck Society
Olivier Maury
Olivier Maury École Normale Supérieure de Lyon
Eckhard Bill
Eckhard Bill Max Planck Society
Xile Hu
Xile Hu École Polytechnique Fédérale de Lausanne
Wolfram Meyer-Klaucke
Wolfram Meyer-Klaucke University of Paderborn
Xiulan Xie
Xiulan Xie Philipp University of Marburg
Yasuo Igarashi
Yasuo Igarashi Southwest University
Thomas Wagner
Thomas Wagner Max Planck Institute for Chemistry
Friedrich Widdel
Friedrich Widdel Max Planck Society

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