Article
Biology
Chris Furlan, Nipa Chongdar, Pooja Gupta, Wolfgang Lubitz, Hideaki Ogata, James N. Blaza, James A. Birrell
Summary: Electron bifurcation is a fundamental energy conservation mechanism in nature that allows endergonic reactions to be driven by exergonic ones. In this study, the structure of HydABC, an electron-bifurcating [FeFe] hydrogenase, was determined using electron cryo-microscopy. The structure revealed a heterododecamer with a central electron transfer pathway, providing insights into the mechanism of electron bifurcation in HydABC. Based on these findings, a possible mechanism of electron bifurcation in HydABC was proposed.
Article
Chemistry, Multidisciplinary
Aurore Jacq-Bailly, Martino Benvenuti, Natalie Payne, Arlette Kpebe, Christina Felbek, Vincent Fourmond, Christophe Leger, Myriam Brugna, Carole Baffert
Summary: Hnd, a tetrameric enzyme from Desulfovibrio fructosovorans, is capable of flavin-based electron bifurcation. Despite its complexity, the enzyme can catalytically exchange electrons with an electrode and demonstrates unique high potential inactivation/reactivation kinetics. The catalytic properties of Hnd are comparable to standard hydrogenases, suggesting that the additional subunits necessary for electron bifurcation do not alter the enzyme's catalytic behavior at the active site.
FRONTIERS IN CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Natalie Payne, Arlette Kpebe, Chloe Guendon, Carole Baffert, Julien Ros, Regine Lebrun, Yann Denis, Laetitia Shintu, Myriam Brugna
Summary: Through studying Desulfovibrio fructosovorans, we discovered that Hnd is involved in ethanol metabolism and oxidizes H-2 via its electron bifurcation mechanism, producing NADH and reduced ferredoxin.
MOLECULAR MICROBIOLOGY
(2022)
Article
Microbiology
Pier Francesco Di Leonardo, Giacomo Antonicelli, Valeria Agostino, Angela Re
Summary: Understanding the organizational and functional properties of hydrogen metabolism is crucial for creating a framework to support a hydrogen-fueled low-carbon economy. This study investigated the genomes of several industrially relevant acetogens and identified their hydrogenases' repertoire. The findings provide valuable knowledge on the functional specificity and potential applications of hydrogenases in biotechnological processes.
MICROBIOLOGY SPECTRUM
(2022)
Article
Microbiology
Gerrit J. Schut, Dominik K. Haja, Xiang Feng, Farris L. Poole, Huilin Li, Michael W. W. Adams
Summary: Microorganisms use electron bifurcating enzymes to carry out unfavorable reactions. The HydABC enzyme is found to be common in the microbial world and has various functionalities. A new class of electron bifurcating enzyme, the Bfu family, is proposed to be associated with specific microbial phyla.
FRONTIERS IN MICROBIOLOGY
(2022)
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, Inorganic & Nuclear
Holly J. Redman, Ping Huang, Michael Haumann, Mun Hon Cheah, Gustav Berggren
Summary: In this study, a molecular mimic of the [FeFe]-hydrogenase was used to explore sustainable sources of hydrogen. Characterization of the produced species was carried out using various spectroscopy techniques. The results revealed the potential of the compound to generate biologically relevant iron-oxidation states and facilitate H-2 gas formation.
DALTON TRANSACTIONS
(2022)
Article
Multidisciplinary Sciences
Anuj Kumar, Florian Kremp, Jennifer Roth, Sven A. Freibert, Volker Mueller, Jan M. Schuller
Summary: This study reports the cryo-EM structure of the Stn class transhydrogenase from Sporomusa ovata and dissects its electron transfer pathway.
NATURE COMMUNICATIONS
(2023)
Review
Chemistry, Physical
James A. Birrell, Patricia Rodriguez-Macia, Adrian Hery-Barranco
Summary: This article introduces how to use infrared spectroscopy and thermodynamic schemes to simulate the redox behaviour of the active site H-cluster in [FeFe] hydrogenases, and discusses the applicability of these models to other metalloenzymes and molecular catalysts.
Article
Chemistry, Physical
Shu-Fen Bai, Jun-Wei Ma, Ya-Nan Guo, Xiu-Mei Du, Yan-Lan Wang, Qian-Li Li, Shuang Lu
Summary: Researchers successfully prepared four types of aminophosphine substituted Fe/E (E = S, Se) carbonyls related to [FeFe]-hydrogenases. These compounds have interesting structures and can be used for electrocatalytic hydrogen production.
JOURNAL OF MOLECULAR STRUCTURE
(2023)
Article
Chemistry, Inorganic & Nuclear
Konstantin Laun, Iuliia Baranova, Jifu Duan, Leonie Kertess, Florian Wittkamp, Ulf-Peter Apfel, Thomas Happe, Moritz Senger, Sven T. Stripp
Summary: [FeFe]-hydrogenases are excellent H-2 evolution catalysts with active site cofactor comprising a [4Fe-4S] cluster linked to a diiron site with carbon monoxide and cyanide ligands. Proton transfer pathways and pH differences affect the stabilization of electrons at different cofactor states, influencing the hydrogen turnover process.
DALTON TRANSACTIONS
(2021)
Review
Chemistry, Multidisciplinary
Adrien Pagnier, Batuhan Balci, Eric M. Shepard, William E. Broderick, Joan B. Broderick
Summary: The assembly and installation of the [FeFe]-hydrogenase H-cluster is not fully understood, but in vitro approaches using semisynthetic and enzyme-based methods have provided new insights into the maturation process. These approaches have shed light on the roles of individual maturation enzymes, the nature of H-cluster assembly intermediates, the molecular precursors of H-cluster ligands, and the sequence of steps involved in [FeFe]-hydrogenase maturation.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2022)
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
Chemistry, Multidisciplinary
Philipp Buday, Chizuru Kasahara, Elisabeth Hofmeister, Daniel Kowalczyk, Micheal K. Farh, Saskia Riediger, Martin Schulz, Maria Wachtler, Shunsuke Furukawa, Masaichi Saito, Dirk Ziegenbalg, Stefanie Grafe, Peter Bauerle, Stephan Kupfer, Benjamin Dietzek-Ivansic, Wolfgang Weigand
Summary: Inspired by natural [FeFe] hydrogenases, a compact and precious metal-free photosensitizer-catalyst dyad (PS-CAT) was designed for photocatalytic hydrogen evolution under visible light. The interaction between PS-CAT and the sacrificial donor was studied through spectroscopy and electrochemical techniques. The formation of an active species was confirmed by operando EPR spectroscopy, driving the photocatalysis effectively (TON approximately 210).
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2022)
Article
Microbiology
Arlette Kpebe, Chloe Guendon, Natalie Payne, Julien Ros, Manel Khelil Berbar, Regine Lebrun, Carole Baffert, Laetitia Shintu, Myriam Brugna
Summary: This study confirms the role of Hnd hydrogenase in ethanol metabolism and uncovers an essential function for a Desulfovibrio hydrogenase for the first time. Hnd is required for S. fructosivorans growth on ethanol, and it produces H-2 from NADH and reduced ferredoxin for ethanol conversion.
FRONTIERS IN MICROBIOLOGY
(2023)
Review
Chemistry, Multidisciplinary
Koji Nishikawa, Hideaki Ogata, Yoshiki Higuchi
Review
Chemistry, Physical
James A. Birrell, Patricia Rodriguez-Macia, Adrian Hery-Barranco
Summary: This article introduces how to use infrared spectroscopy and thermodynamic schemes to simulate the redox behaviour of the active site H-cluster in [FeFe] hydrogenases, and discusses the applicability of these models to other metalloenzymes and molecular catalysts.
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
Maria Alessandra Martini, Olaf Ruediger, Nina Breuer, Birgit Noering, Serena DeBeer, Patricia Rodriguez-Macia, James A. Birrell
Summary: FeFe hydrogenases are highly active enzymes that catalyze proton and electron interconversion with hydrogen. Their active site consists of a [4Fe-4S] cluster and a [2Fe] subcluster, with the former storing electrons and the latter responsible for hydrogen splitting and formation. Investigating the catalytic mechanism reveals the presence of various models, with one suggesting the involvement of an alternative oxidized state, HoxH, under certain conditions.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2021)
Article
Biochemical Research Methods
Takahiro Imanishi, Koji Nishikawa, Midori Taketa, Katsuhiro Higuchi, Hulin Tai, Shun Hirota, Hironobu Hojo, Toru Kawakami, Kiriko Hataguchi, Kayoko Matsumoto, Hideaki Ogata, Yoshiki Higuchi
Summary: This study investigated the binding state of CO with the hydrogenase in Citrobacter sp. S-77 using activity assays, spectroscopic techniques, and X-ray crystallography. The results showed a positive correlation between CO tolerance and oxygen tolerance in [NiFe]-hydrogenases.
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
(2022)
Review
Chemistry, Multidisciplinary
Sven T. Stripp, Benjamin R. Duffus, Vincent Fourmond, Christophe Leger, Silke Leimkueshler, Shun Hirota, Yilin Hu, Andrew Jasniewski, Hideaki Ogata, Markus W. Ribbe
Summary: Gases like H-2, N-2, CO2, and CO are important feedstock for green energy conversion and as sources of nitrogen and carbon. However, their industrial transformation and production require significant energy input, whereas nature efficiently converts them at ambient conditions using gas-processing metalloenzymes (GPMs). In this review, the importance of the cofactor/protein interface in GPMs is emphasized, and the effects of second and outer coordination sphere on catalytic activity are discussed.
Article
Nanoscience & Nanotechnology
Jana M. Becker, Anna Lielpetere, Julian Szczesny, Joao R. C. Junqueira, Patricia Rodriguez-Macia, James A. Birrell, Felipe Conzuelo, Wolfgang Schuhmann
Summary: The development of electrodes for efficient CO2 reduction is crucial, and the use of enzymes as catalysts offers high catalytic activity and selectivity. In this study, a bioelectrode using a low-potential redox polymer was used for the selective reduction of CO2 to CO, achieving high catalytic current densities and good stability.
ACS APPLIED MATERIALS & INTERFACES
(2022)
Article
Biology
Chris Furlan, Nipa Chongdar, Pooja Gupta, Wolfgang Lubitz, Hideaki Ogata, James N. Blaza, James A. Birrell
Summary: Electron bifurcation is a fundamental energy conservation mechanism in nature that allows endergonic reactions to be driven by exergonic ones. In this study, the structure of HydABC, an electron-bifurcating [FeFe] hydrogenase, was determined using electron cryo-microscopy. The structure revealed a heterododecamer with a central electron transfer pathway, providing insights into the mechanism of electron bifurcation in HydABC. Based on these findings, a possible mechanism of electron bifurcation in HydABC was proposed.
Article
Chemistry, Multidisciplinary
Nipa Chongdar, Patricia Rodriguez-Macia, Edward J. Reijerse, Wolfgang Lubitz, Hideaki Ogata, James A. Birrell
Summary: This study investigates the influence of the protein environment on the catalytic, spectroscopic, and redox properties of [FeFe] hydrogenases. Mutations at the non-conserved serine 267 site resulted in a significant decrease in activity and a lower redox potential for the [4Fe-4S] subcluster. These findings highlight the important role of the secondary coordination sphere in tuning the catalytic properties of [FeFe] hydrogenases.
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
Rhiannon M. Evans, Stephen E. Beaton, Patricia Rodriguez Macia, Yunjie Pang, Kin Long Wong, Leonie Kertess, William K. Myers, Ragnar Bjornsson, Philip A. Ash, Kylie A. Vincent, Stephen B. Carr, Fraser A. Armstrong
Summary: A variant of hydrogenase-2 from E. coli with a mutated arginine residue at its active site forms a tightly-bound diatomic ligand. This ligand is stabilized by hydrogen bonding and removal only occurs after reduction with H-2 and reduced methyl viologen. The R479K variant shows decreased rates in hydrogen oxidation and evolution compared to the native enzyme. Importance rating: 7/10.
Article
Chemistry, Multidisciplinary
Marco Lorenzi, Joe Gellett, Afridi Zamader, Moritz Senger, Zehui Duan, Patricia Rodriguez-Macia, Gustav Berggren
Summary: Artificial maturation of hydrogenases provides a path to generate semi-synthetic enzymes with novel catalytic properties. This study prepared enzymes containing a synthetic asymmetric mono-cyanide cofactor and investigated their structure and reactivity. The choice of host enzyme was found to have a significant impact on reactivity, and the study showed that synthetic manipulations of the active-site can increase inhibitor tolerance.
