Article
Chemistry, Multidisciplinary
Christian Lorent, Vladimir Pelmenschikov, Stefan Frielingsdorf, Janna Schoknecht, Giorgio Caserta, Yoshitaka Yoda, Hongxin Wang, Kenji Tamasaku, Oliver Lenz, Stephen P. Cramer, Marius Horch, Lars Lauterbach, Ingo Zebger
Summary: A new experimental setup was developed to study metalloenzymes in detail, allowing the controlled preparation and characterization of catalytic intermediates using various spectroscopic techniques. By investigating two O-2-tolerant [NiFe]-hydrogenases as model systems, detailed insights into the catalytic mechanisms and vibrational fingerprints were revealed. Additionally, the study highlighted the importance of complementing X-ray crystallographic data with spectroscopic analyses.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Article
Multidisciplinary Sciences
Rhiannon M. Evans, Natalie Krahn, Bonnie J. Murphy, Harrison Lee, Fraser A. Armstrong, Dieter Soll
Summary: The study investigates the impact of substituting cysteine with selenocysteine on the function of [NiFe]-hydrogenases, revealing that while the activity of the enzymes is reduced after substitution, variants with selenocysteine show significant differences in O-2 tolerance and electrocatalytic properties.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2021)
Article
Chemistry, Multidisciplinary
Ravi Kumar, Matthias Stein
Summary: Recently, it was discovered that the oxygen tolerance of the [NiFe]-hydrogenase from H. thermoluteolus stems from an unusual coordination sphere of the active site nickel atom. In the oxidized state, a terminal cysteine residue is displaced by a bidentate coordinating nearby glutamate, resulting in its occupation of a third bridging position.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Chemistry, Applied
Gabriel Luna-Lopez, Raquel Sainz, Ana M. Coito, Charlotte Pichon, Ana Iglesias-Juez, Ines A. C. Pereira, Antonio L. De Lacey, Marcos Pita
Summary: In order to tackle the challenge of diminishing the high potentials required for the reaction, a combination of a redox biocatalyst and an inorganic semiconductor has been studied. The system, based on a photocathode made of copper gallium sulfide and Desulfovibrio vulgaris Hildenborough NiFeSe-hydrogenase, can produce photoelectrochemical biocatalytic proton reduction to H2 without any sacrificial agent while providing an approximately 400 mV decrease of the applied potential.
Article
Chemistry, Multidisciplinary
Catharina J. Kulka-Peschke, Anne-Christine Schulz, Christian Lorent, Yvonne Rippers, Stefan Wahlefeld, Janina Preissler, Claudia Schulz, Charlotte Wiemann, Cornelius C. M. Bernitzky, Chara Karafoulidi-Retsou, Solomon L. D. Wrathall, Barbara Procacci, Hiroaki Matsuura, Gregory M. Greetham, Christian Teutloff, Lars Lauterbach, Yoshiki Higuchi, Masaharu Ishii, Neil T. Hunt, Oliver Lenz, Ingo Zebger, Marius Horch
Summary: The NAD(+)-reducing [NiFe] hydrogenase from Hydrogenophilus thermoluteolus shows promising potential for biotechnological applications due to its O2 tolerance and thermostability. Through studying the active-site structure and catalytic activity of native HtSH and its variants, it was revealed that oxidized HtSH features unusual active-site states with unique responses to O2, potentially serving as a mechanism to protect the enzyme from oxidative damage.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Article
Chemistry, Inorganic & Nuclear
Li-Cheng Song, Yin-Peng Wang, Yi-Xiong Dong, Xi-Yue Yang
Summary: A series of new biomimetics for the active site of [NiFe]-H(2)ases have been prepared using various synthetic methods. These biomimetics can catalyze proton reduction to generate hydrogen and undergo a range of chemical reactions.
DALTON TRANSACTIONS
(2023)
Article
Biochemistry & Molecular Biology
Gabriel Luna-Lopez, Melisa del Barrio, Jennifer Fize, Vincent Artero, Ana Margarida Coito, Ines A. C. Pereira, Jose Carlos Conesa, Ana Iglesias-Juez, Antonio L. De Lacey, Marcos Pita
Summary: Clean energy vectors are required to achieve a fossil fuel-free society, reducing both greenhouse effect and pollution. Electrochemical water splitting provides a clean method to obtain green hydrogen, but efficient electrocatalysts are needed to avoid high overpotentials. The combination of inorganic semiconductors with biocatalysts offers an alternative approach for photoelectrochemical H2 production.
BIOELECTROCHEMISTRY
(2023)
Article
Chemistry, Physical
Haruhiko Teramoto, Tetsu Shimizu, Masako Suda, Masayuki Inui
Summary: This study explored the genetic engineering of Escherichia coli for hydrogen production. The introduction of exogenous hydrogenase and inactivation of endogenous hydrogenases resulted in both hydrogen production and uptake. Disabling the pathways for ethanol, lactate, and succinate production significantly increased hydrogen production. Unexpectedly, high expression of exogenous hydrogenase completely repressed hydrogen production, and the introduction of heterologous enzyme repressed the endogenous hydrogen production ability.
INTERNATIONAL JOURNAL OF HYDROGEN ENERGY
(2022)
Article
Materials Science, Biomaterials
Qiuyao Jiang, Tianpei Li, Jing Yang, Catherine M. Aitchison, Jiafeng Huang, Yu Chen, Fang Huang, Qiang Wang, Andrew I. Cooper, Lu-Ning Liu
Summary: Researchers engineered the protein organelle in bacteria cells to encapsulate hydrogenases, resulting in improved hydrogen production and catalytic efficiency. This study provides a framework for developing new bio-inspired electrocatalysts for sustainable fuel and chemical production.
JOURNAL OF MATERIALS CHEMISTRY B
(2023)
Article
Chemistry, Multidisciplinary
Birgit Fuchs, Dirk Johrendt, Lkhamsuren Bayarjargal, Hubert Huppertz
Summary: CrB4O6N crystallizes in a non-centrosymmetric space group and is the first high-pressure oxonitridoborate. It consists of starlike-shaped entities of four BO3N tetrahedra connected via one common nitrogen atom, and contains a tetrahedral building unit in contrast to other oxonitridoborates.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Article
Chemistry, Multidisciplinary
Hui-Jie Pan, Gangfeng Huang, Matthew D. Wodrich, Farzaneh Fadaei Tirani, Kenichi Ataka, Seigo Shima, Xile Hu
Summary: The study discusses the reconstitution of [Mn]-hydrogenases using Mn-I complexes, highlighting the importance of internal base or pro-base in catalysis. The results confirm the essential role of metal-ligand cooperation for H-2 activation and indicate differences in the mode of cooperation between active [Mn]-hydrogenases and native [Fe]-hydrogenase. This work demonstrates the possibility of reconstituting active artificial hydrogenases using synthetic complexes.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Review
Chemistry, Inorganic & Nuclear
James A. Birrell, Patricia Rodriguez-Macia, Edward J. Reijerse, Maria Alessandra Martini, Wolfgang Lubitz
Summary: This review provides an overview of the research history and progress on hydrogenases, focusing on their structure, mechanism of action, and catalytic cycle. It compares the studies on the simple enzyme containing the active site H-cluster and enzymes containing additional iron-sulfur clusters.
COORDINATION CHEMISTRY REVIEWS
(2021)
Article
Chemistry, Multidisciplinary
Armel F. T. Waffo, Christian Lorent, Sagie Katz, Janna Schoknecht, Oliver Lenz, Ingo Zebger, Giorgio Caserta
Summary: This study used cryogenic infrared and electron paramagnetic resonance spectroscopy to decipher the structural basis of the Ni-a-L intermediates in the regulatory [NiFe]-hydrogenase from Cupriavidus necator, revealing the importance of the protein scaffold in fine-tuning proton and electron dynamics.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Chemistry, Multidisciplinary
Takeshi Hiromoto, Koji Nishikawa, Seiya Inoue, Hideaki Ogata, Yuta Hori, Katsuhiro Kusaka, Yu Hirano, Kazuo Kurihara, Yasuteru Shigeta, Taro Tamada, Yoshiki Higuchi
Summary: This study reports that [NiFe]-hydrogenase from Desulfovibrio vulgaris Miyazaki F can recover its catalytic activity by reacting with H2 under anaerobic conditions after being inactivated in the presence of O2. Neutron structure analysis revealed that a part of the Ni ion dissociates from the active site Ni-Fe complex and forms a new square-planar Ni complex, accompanied by rearrangement of the coordinated thiolate ligands. The analysis also found that the Cys17(S) thiolate forms an unusual hydrogen bond with the main-chain amide N atom of Gly19(S), providing insights into the redox reaction of the Fe-S cluster.
Article
Chemistry, Multidisciplinary
Andrea Schmidt, Jacqueline Kalms, Christian Teutloff, Sagie Katz, Stefan Frielingsdorf, Rhiannon M. Evans, Johannes Fritsch, Elisabeth Siebert, Christian Teutloff, Fraser A. Armstrong, Ingo Zebger, Oliver Lenz, Patrick Scheerer
Summary: The membrane-bound [NiFe]-hydrogenase of Cupriavidus necator is an O-2-tolerant hydrogenase with a unique Cys(6)[4Fe-3S] cluster. Replacing two additional cysteines in the cluster led to structural changes and decreased O-2 tolerance. Formation of a hydroxy ligand in the active site under electron-deficient conditions can protect the enzyme from O-2 binding.
Article
Chemistry, Multidisciplinary
Christian Lorent, Vladimir Pelmenschikov, Stefan Frielingsdorf, Janna Schoknecht, Giorgio Caserta, Yoshitaka Yoda, Hongxin Wang, Kenji Tamasaku, Oliver Lenz, Stephen P. Cramer, Marius Horch, Lars Lauterbach, Ingo Zebger
Summary: A new experimental setup was developed to study metalloenzymes in detail, allowing the controlled preparation and characterization of catalytic intermediates using various spectroscopic techniques. By investigating two O-2-tolerant [NiFe]-hydrogenases as model systems, detailed insights into the catalytic mechanisms and vibrational fingerprints were revealed. Additionally, the study highlighted the importance of complementing X-ray crystallographic data with spectroscopic analyses.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Article
Chemistry, Multidisciplinary
Shenglai Yao, Arseni Kostenko, Yun Xiong, Christian Lorent, Ales Ruzicka, Matthias Driess
Summary: Using a chelating C,C'-bis(silylenyl)-ortho-dicarborane ligand, a monoatomic zero-valent Ge complex was synthesized, showing different reactivities towards reductants and oxidants due to the redox non-innocent nature of the carborane scaffold. The reduction and oxidation of the Ge complex resulted in the formation of dianionic or dicationic bis(silylene)-supported Ge complexes with distinct properties.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Article
Microbiology
Qin Fan, Giorgio Caserta, Christian Lorent, Oliver Lenz, Peter Neubauer, Matthias Gimpel
Summary: Hydrogenases are important metalloenzymes that have witnessed significant progress in recent years, albeit with difficulties in low production yields. By heterologously expressing the hydrogenase RH, its yield was substantially increased and single subunits were successfully overproduced, offering a new strategy for bioprocess development and structural studies.
Article
Chemistry, Multidisciplinary
Jae-Hun Jeoung, Jochen Fesseler, Lilith Domnik, Friederike Klemke, Malte Sinnreich, Christian Teutloff, Holger Dobbek
Summary: This study reports on the structure and reactivity of an aberrant enzyme, CooS-V-Ch. Despite its close relation to CODHs, CooS-V-Ch undergoes a restructuring of its active site and contains an iron-sulfur-oxo hybrid-cluster. It does not catalyze CO oxidation or CO2 reduction.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2022)
Article
Biochemistry & Molecular Biology
Elisabeth Lettau, Domenic Zill, Marta Spaeth, Christian Lorent, Praveen K. Singh, Lars Lauterbach
Summary: This study presents the biochemical and spectroscopic characteristics of the reductase MmoC from the marine methanotroph Methylomonas methanica MC09. The presence of flavin adenine dinucleotide and [2Fe2S] cluster as prosthetic groups in MmoC was revealed. MmoC showed good halotolerance and high activity, which is important for future biotechnological applications of halotolerant soluble methane monooxygenase.
Article
Chemistry, Inorganic & Nuclear
Jae-Hun Jeoung, Stefan Runger, Michael Haumann, Bettina Neumann, Friederike Klemke, Victoria Davis, Anna Fischer, Holger Dau, Ulla Wollenberger, Holger Dobbek
Summary: The study compared four homobimetallic cofactors reconstituted into a four-helix bundle protein, revealing variations in their reaction rates and product structures despite high affinity binding and similar structures. Changing the metal composition offers opportunities to modulate the reactivity of bimetallic cofactors and study functionalize reactive species.
INORGANIC CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Domenic Zill, Elisabeth Lettau, Christian Lorent, Franziska Seifert, Praveen K. Singh, Lars Lauterbach
Summary: Researchers have successfully heterologously produced active sMMO, an enzyme that can convert methane to methanol, in Escherichia coli. This study enables the expansion of detailed studies on sMMO and opens up possibilities for novel biotechnological applications.
Article
Microbiology
Qin Fan, Giorgio Caserta, Christian Lorent, Ingo Zebger, Peter Neubauer, Oliver Lenz, Matthias Gimpel
Summary: In this study, the production process of heterologous hydrogenase in E. coli was significantly improved to obtain catalytically active regulatory hydrogenase (RH). Important factors such as O-2 content, metal availability, production conditions, and co-expression of RH-specific maturase genes were optimized. The maturation of RH was successfully achieved during aerobic cultivation of E. coli by co-production of seven hydrogenase-specific maturases and a nickel permease. The improved production conditions resulted in a high yield of catalytically active RH and an increased space-time yield in E. coli compared to the native host C. necator. This strategy has important implications for the production of catalytically active [NiFe]-hydrogenases in biotechnologically relevant quantities.
FRONTIERS IN MICROBIOLOGY
(2022)
Article
Multidisciplinary Sciences
Jae-Hun Jeoung, Sabine Nicklisch, Holger Dobbek
Summary: Metalloenzymes coupled with ATP hydrolysis can catalyze reductions at very negative reduction potentials. The study found that the DCCP:DCCP-R complex forms stable complexes and facilitates ATP-driven electron transfer through structural changes and hydrogen bond networks.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2022)
Article
Chemistry, Physical
Yudhajeet Basak, Jae-Hun Jeoung, Lilith Domnik, Jakob Ruickoldt, Holger Dobbek
Summary: Carbon monoxide dehydrogenases catalyze the reversible conversion of CO and water. Highly conserved amino acids in the second coordination sphere of cluster C support substrate activation and catalytic turnover.
Article
Chemistry, Physical
Jakob Ruickoldt, Yudhajeet Basak, Lilith Domnik, Jae-Hun Jeoung, Holger Dobbek
Summary: The kinetic characterization of three CODHases with distinct physiological roles revealed insights into the rate-determining steps in catalysis and allowed modeling the influence of the reduction potential of the electron-transferring clusters on catalysis. Potential clues for the different activities of the CODHases were investigated, with a point mutation doubling the activity of one complex, indicating that the architecture of the substrate tunnels may be the main reason for the different activities.
Article
Chemistry, Physical
Yvonne Rippers, Barbara Procacci, Neil T. Hunt, Marius Horch
Summary: This study presents a computational approach for simulating and analyzing static 2D-IR spectra of [NiFe] hydrogenases and similar organometallic systems. By accurately reproducing experimental spectra, it reveals the crucial role of the [NiFe] core in shaping the enzymatic potential energy surface and provides molecular information not accessible by experiments.
Article
Chemistry, Multidisciplinary
Maria Alessandra Martini, Konstantin Bikbaev, Yunjie Pang, Christian Lorent, Charlotte Wiemann, Nina Breuer, Ingo Zebger, Serena DeBeer, Ingrid Span, Ragnar Bjornsson, James A. Birrell, Patricia Rodriguez-Macia
Summary: [FeFe] hydrogenase variants with a mutation in the proton transfer pathway can form two new active site states with a CN- ligand bound to the apical position of [2Fe](H). These states can be generated by either cannibalization from damaged [2Fe](H) subclusters or addition of exogenous CN-. This study provides the first detailed characterization of the interaction between exogenous CN- and [FeFe] hydrogenases.
Article
Chemistry, Physical
Solomon L. D. Wrathall, Barbara Procacci, Marius Horch, Emily Saxton, Chris Furlan, Julia Walton, Yvonne Rippers, James N. Blaza, Gregory M. Greetham, Michael Towrie, Anthony W. Parker, Jason Lynam, Alison Parkin, Neil T. Hunt
Summary: Ultrafast two-dimensional infrared spectroscopy was used to study the structural and dynamic influence of the protein scaffold on the Fe(CO)(CN)(2) unit of the active site of Escherichia coli Hyd-1 (EcHyd-1). New active site states were observed and assigned using 2D-IR, and the vibrational levels and relaxation dynamics of the CO and CN modes were determined. The results show that the protein scaffold creates a distinct biomolecular environment for the NiFe site that differs from simple models of solvation.
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
(2022)
Article
Chemistry, Multidisciplinary
Giorgio Caserta, Vladimir Pelmenschikov, Christian Lorent, Armel F. Tadjoung Waffo, Sagie Katz, Lars Lauterbach, Janna Schoknecht, Hongxin Wang, Yoshitaka Yoda, Kenji Tamasaku, Martin Kaupp, Peter Hildebrandt, Oliver Lenz, Stephen P. Cramer, Ingo Zebger
Summary: Understanding the relationship between [NiFe]-hydrogenases and their resting states is crucial for elucidating their catalytic mechanism and enzymatic activity.