Article
Chemistry, Multidisciplinary
Claudia Brocks, Chandan K. Das, Jifu Duan, Shanika Yadav, Ulf-Peter Apfel, Subhasri Ghosh, Eckhard Hofmann, Martin Winkler, Vera Engelbrecht, Lars V. Schaefer, Thomas Happe
Summary: This study proposes a new strategy to improve the O-2 stability of [FeFe]-hydrogenases by blocking the O-2 diffusion pathway and protecting the catalytic cofactor.
Article
Chemistry, Physical
Andreas Rutz, Chandan K. Das, Andrea Fasano, Jan Jaenecke, Shanika Yadav, Ulf-Peter Apfel, Vera Engelbrecht, Vincent Fourmond, Christophe Leger, Lars Schaefer, Thomas Happe
Summary: The active site of [FeFe]-hydrogenases degrades upon contact with oxygen, but the protein structure of a certain hydrogenase (CbA5H) allows its active site to be protected, reducing degradation caused by oxygen. By modifying the surface residue, the hydrogenase's resistance to oxygen can be increased.
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, Physical
Monica L. K. Sanchez, Seth Wiley, Edward Reijerse, Wolfgang Lubitz, James A. Birrell, R. Brian Dyer
Summary: The FeFe hydrogenases are efficient catalysts for hydrogen conversion, with a unique active site containing a [4Fe-4S] electron relay and a diiron cluster ligated by CO, CN-, and ADT ligands. The study using TRIR spectroscopy on the CrHydA1 hydrogenase revealed that a modification with PDT ligand inhibits the enzyme from proceeding through the catalytic cycle. The results suggest that the first electron transfer step is pH-independent, supporting a simple electron transfer mechanism rather than a proton-coupled event.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2022)
Article
Chemistry, Inorganic & Nuclear
Shuang Lu, Cui-Rong Qin, Hui-Lin Ma, Ji-Min Ouyang, Qian-Li Li
Summary: Two electron-rich, PR3-disubstituted diiron bis(monothiolate) carbonyls were prepared as biomimetic models of the active site of [FeFe]-H(2)ases. Mu-hydride diiron compounds were also synthesized as structural and functional models for the protonated diiron subsite. Characterization and electrochemical property studies were conducted for all compounds, with one compound found to catalyze H-2 production in the presence of acetic acid.
INORGANICA CHIMICA ACTA
(2021)
Article
Chemistry, Multidisciplinary
Melanie Heghmanns, Andreas Rutz, Yury Kutin, Vera Engelbrecht, Martin Winkler, Thomas Happe, Muege Kasanmascheff
Summary: In this study, the active center of CbA5H, the H-cluster, was characterized using multifrequency continuous wave and pulsed electron paramagnetic resonance spectroscopy. It was found that under oxidizing conditions, an additional radical species dominates the spectra. The generation of this radical signal depends on the presence of an intact H-cluster and a complete proton transfer pathway.
Article
Chemistry, Multidisciplinary
Carolyn E. Lubner, Jacob H. Artz, David W. Mulder, Aisha Oza, Rachel J. Ward, S. Garrett Williams, Anne K. Jones, John W. Peters, Ivan I. Smalyukh, Vivek S. Bharadwaj, Paul W. King
Summary: Redox cofactors play a crucial role in mediating electron transfer in biological enzymes. One example is the [FeFe]-hydrogenase I from Clostridium acetobutylicum, which utilizes a terminal, non-canonical, His-coordinated, [4Fe-4S] cluster to mediate interfacial electron transfer. Substituting His for Cys in this enzyme results in changes in electron transfer properties and reactivity, demonstrating the importance of His coordination in controlling electron exchange.
Article
Chemistry, Inorganic & Nuclear
Simone Morra, Jifu Duan, Martin Winkler, Philip A. Ash, Thomas Happe, Kylie A. Vincent
Summary: By maintaining individual crystals of [FeFe]-hydrogenase under electrochemical control and probing them via Fourier Transform Infrared (FTIR) microspectroscopy, it is possible to precisely tune the redox potential and reveal variations in the distribution of redox states at the active site. This approach offers high sensitivity and precise redox control, facilitating the detection and characterisation of low abundance species and new redox intermediates within a narrow window of conditions.
DALTON TRANSACTIONS
(2021)
Article
Microbiology
Effie C. Kisgeropoulos, Vivek S. Bharadwaj, David W. Mulder, Paul W. King
Summary: The preferences for H-2 oxidation or H-2 production reactions vary among different groups of [FeFe]-hydrogenases. The pKa of the proton-transfer residue plays a significant role in controlling reactivity, with a change from cysteine to serine favoring H-2 oxidation and a change to aspartate causing a shift towards H-2 evolution. The effect of changing the proton-transfer residue pKa can be explained in terms of the scaling relationship between the H-cluster ligand pKa and E-m values.
FRONTIERS IN MICROBIOLOGY
(2022)
Article
Chemistry, Multidisciplinary
Moritz Senger, Tobias Kernmayr, Marco Lorenzi, Holly J. Redman, Gustav Berggren
Summary: This study reveals that small molecules in solution can interfere with mechanistic investigations by affecting the stability of catalytic states and producing off-cycle states. The researchers demonstrate the formation of the hydride state in wild-type [FeFe]-hydrogenases treated with H-2 and discover a new state induced by common low pH buffers, the role of which in catalysis remains unclear.
CHEMICAL COMMUNICATIONS
(2022)
Article
Chemistry, Inorganic & Nuclear
Eric M. Shepard, Stella Impano, Benjamin R. Duffus, Adrien Pagnier, Kaitlin S. Duschene, Jeremiah N. Betz, Amanda S. Byer, Amanda Galambas, Elizabeth C. McDaniel, Hope Watts, Shawn E. McGlynn, John W. Peters, William E. Broderick, Joan B. Broderick
Summary: The study demonstrates that Clostridium acetobutylicum HydG catalyzes the formation of multiple equivalents of free CO and CN-, and suggests that the dangler iron is not essential but may affect relevant catalysis. Free CO/CN- are essential species in hydrogenase maturation.
DALTON TRANSACTIONS
(2021)
Article
Chemistry, Physical
Ahmad Q. Daraosheh, Hassan Abul-Futouh, Natsuki Murakami, Karl Michael Ziems, Helmar Goerls, Stephan Kupfer, Stefanie Graefe, Akihiko Ishii, Malgorzata Celeda, Grzegorz Mloston, Wolfgang Weigand
Summary: The influence of substitution pattern in ferrocenyl alpha-thienyl thioketone as a proligand in complexation reactions with Fe-3(CO)(12) was investigated, resulting in the synthesis of two new sulfur-iron complexes. These complexes were found to catalyze the reduction of protons to molecular hydrogen, and the presence of the ferrocene moiety improved the stability of the reduced species.
Review
Chemistry, Multidisciplinary
David W. Mulder, John W. Peters, Simone Raugei
Summary: Catalytic bias refers to the propensity of a reaction catalyst to accelerate the rate of reaction differently in one direction versus the other under non-equilibrium conditions. Enzyme's inherent bias in biocatalysis is advantageous for promoting efficiency and coordination, while directional catalytic bias is sought after in industrial chemical catalysis.
CHEMICAL COMMUNICATIONS
(2021)
Article
Chemistry, Physical
Victoria Davis, Nina Heidary, Amandine Guiet, Khoa Hoang Ly, Maximilian Zerball, Claudia Schulz, Norbert Michael, Regine von Klitzing, Peter Hildebrandt, Stefan Frielingsdorf, Oliver Lenz, Ingo Zebger, Anna Fischer
Summary: The oxygen tolerance of membrane-bound [NiFe] hydrogenase (MBH) from Cupriavidus necator makes it an attractive electrocatalyst for hydrogen energy conversion devices. By immobilizing MBH with affinity tags on a tin-rich indium tin oxide (ITOTR) electrode, hydrogen oxidation and an unusually high proton reduction current were observed, suggesting bidirectionality in unidirectional [NiFe] hydrogenases. The favorable enzyme-semiconductor interactions contribute to this behavior.
Article
Chemistry, Physical
Mario Gallego, Avelino Corma, Mercedes Boronat
Summary: The reactivity towards O-2 dissociation of Cu-5 and Cu-7 clusters confined within the CHA zeolite cavities is investigated, and it is found that the Si/Al ratio in the zeolite support can finely tune the stability and oxidation properties of Cu-based catalysts.
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
(2022)
Article
Chemistry, Multidisciplinary
Marta Meneghello, Alexandre Uzel, Marianne Broc, Rita R. Manuel, Axel Magalon, Christophe Leger, Ines A. C. Pereira, Anne Walburger, Vincent Fourmond
Summary: Metal-based formate dehydrogenases are enzymes that require molybdenum or tungsten ions to catalyze the conversion between formate and CO2. The coordination of the metal ion in the active form prevents direct binding of formate to the metal. The study's findings provide strong evidence for the hypothesis that the oxidation of formate occurs in the second coordination sphere of the metal.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)
Article
Chemistry, Inorganic & Nuclear
Vladimir Pelmenschikov, Chien-Hong Chen, I-Jui Hsu, Ulf-Peter Apfel, Giorgio Caserta, Lars Lauterbach, Tsai-Te Lu, Yu-Ting Tseng, Linda Iffland-Mu''hlhaus, Donato Calabrese, Yu-Che Chang, Konstantin Laun, Chih-Wen Pao, Ilya Sergueev, Yoshitaka Yoda, Wen-Feng Liaw
Summary: Efforts are being made to develop earth-abundant metal catalysts for dehydrogenation/hydrolysis of amine boranes. In this study, complex 3-K-crown was explored as a pre-catalyst for the dehydrogenation of DMAB, and the transformation of 3-K-crown into intermediate A during H-2 generation was supported by experimental and computational results. The substrate-gated transformation of pre-catalyst 3 into intermediate A was also observed in the reaction of complex 4-Na-crown with CO as an alternative synthetic route.
INORGANIC CHEMISTRY
(2023)
Article
Biochemistry & Molecular Biology
Giorgio Caserta, Sven Hartmann, Casey Van Stappen, Chara Karafoulidi-Retsou, Christian Lorent, Stefan Yelin, Matthias Keck, Janna Schoknecht, Ilya Sergueev, Yoshitaka Yoda, Peter Hildebrandt, Christian Limberg, Serena DeBeer, Ingo Zebger, Stefan Frielingsdorf, Oliver Lenz
Summary: In this study, the maturation process of [NiFe]-hydrogenase was investigated using biochemical analysis and various spectroscopic techniques, providing detailed insights into its complex maturation mechanism.
NATURE CHEMICAL BIOLOGY
(2023)
Article
Chemistry, Physical
Andreas Rutz, Chandan K. Das, Andrea Fasano, Jan Jaenecke, Shanika Yadav, Ulf-Peter Apfel, Vera Engelbrecht, Vincent Fourmond, Christophe Leger, Lars Schaefer, Thomas Happe
Summary: The active site of [FeFe]-hydrogenases degrades upon contact with oxygen, but the protein structure of a certain hydrogenase (CbA5H) allows its active site to be protected, reducing degradation caused by oxygen. By modifying the surface residue, the hydrogenase's resistance to oxygen can be increased.
Article
Microbiology
Jovan Dragelj, Chara Karafoulidi-Retsou, Sagie Katz, Oliver Lenz, Ingo Zebger, Giorgio Caserta, Sophie Sacquin-Mora, Maria Andrea Mroginski
Summary: In this study, the conformational and mechanical stability of the large subunit HoxG of the membrane-bound hydrogenase from Cupriavidus necator (CnMBH) was investigated using molecular modelling and molecular dynamics simulations. The simulations revealed that isolated HoxG is stable in aqueous solution and preserves a large portion of its mechanical properties, but loses rigidity around the active site. However, regained rigidity was observed in homodimer models. Furthermore, the simulations showed significant positive charge at the protein surface, especially in solvent-exposed former dimer interfaces.
FRONTIERS IN MICROBIOLOGY
(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, Inorganic & Nuclear
Cheriehan Hessin, Jules Schleinitz, Nolwenn Le Breton, Sylvie Choua, Laurence Grimaud, Vincent Fourmond, Marine Desage-El Murr, Christophe Leger
Summary: Potential inversion refers to the phenomenon where the second electron transfer is easier than the first, and it is significant for understanding enzyme catalysis and developing efficient catalysts. Currently, there is a lack of analytical predictions to interpret voltammetric peak potentials when potential inversion occurs, and cyclic voltammograms are often analyzed without considering overfitting or estimating error. In this study, a theory for voltammetry of two-electron redox species in the irreversible limit is formulated and applied to analyze the voltammetry of a nickel complex with redox-active ligands, highlighting the intrinsic underdetermination of the model. Characterizing the thermodynamics of two-electron electron-transfer reactions is crucial for catalyst design.
INORGANIC CHEMISTRY
(2023)
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
Raphael J. Labidi, Bruno Faivre, Philippe Carpentier, Giulia Veronesi, Albert Solei-Daura, Ragnar Bjornsson, Christophe Leïger, Philipp Gotico, Yun Li, Mohamed Atta, Marc Fontecave
Summary: In this study, the performance of the orange protein (Orp) as a catalyst for photocatalytic reduction of protons into H-2 under visible light irradiation was investigated. It was found that Orp exhibited excellent photocatalytic activity in the presence of ascorbate as the sacrificial electron donor and [Ru(bpy)(3)]Cl-2 as the photosensitizer. Density functional theory (DFT) calculations were used to propose a consistent reaction mechanism.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Correction
Chemistry, Multidisciplinary
Vincent Fourmond, Carole Baffert, Kateryna Sybirna, Thomas Lautier, Abbas Abou Hamdan, Sebastien Dementin, Philippe Soucaille, Isabelle Meynial-Salles, Herve Bottin, Christophe Leger
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Chemistry, Multidisciplinary
Andrea Fasano, Chloe Guendon, Aurore Jacq-Bailly, Arlette Kpebe, Jeremy Wozniak, Carole Baffert, Melisa del Barrio, Vincent Fourmond, Myriam Brugna, Christophe Leger
Summary: The observation that some homologous enzymes have the same active site but very different catalytic properties demonstrates the importance of long-range effects in enzyme catalysis. In this study, the catalytic bias and sensitivity of hydrogenase 1 (Hyd 1) were found to be determined by the catalytic subunit rather than the electron transfer chain, and the proximal cluster was confirmed to play a role in the enzyme's resistance to long-term exposure to O-2. This research provides insights into the structure-function relationships of hydrogenases and offers possibilities for engineering useful hydrogenases with desired properties.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Correction
Chemistry, Multidisciplinary
Vincent Fourmond, Carole Baffert, Kateryna Sybirna, Thomas Lautier, Abbas Abou Hamdan, Philippe Soucaille, Isabelle Meynial-Salles, Christophe Leger
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
