Review
Microbiology
Simone Morra
Summary: FeFe-hydrogenases are complex metalloenzymes that play a key role in microbial energy metabolism. They use protons from water as terminal electron acceptors to dissipate excess reducing equivalents and produce hydrogen. FeFe-hydrogenases also have additional physiological functions, such as H-2 uptake, H-2 sensing, and CO2 fixation. Recent advancements in identifying and characterising novel FeFe-hydrogenases have expanded our understanding of their multiple roles and mechanisms.
FRONTIERS IN MICROBIOLOGY
(2022)
Article
Chemistry, Multidisciplinary
Roman Rohac, Lydie Martin, Liang Liu, Debashis Basu, Lizhi Tao, R. David Britt, Thomas B. Rauchfuss, Yvain Nicolet
Summary: FeFe-hydrogenases use a unique H cluster to convert H-2 into protons and low-potential electrons. The [2Fe](H) center is where the reaction occurs and is built stepwise by maturating enzymes, with HydE performing complex modifications of complex-B to produce a precursor to the [2Fe](H) center.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2021)
Article
Chemistry, Multidisciplinary
Yu Zhang, Lizhi Tao, Toby J. Woods, R. David Britt, Thomas B. Rauchfuss
Summary: This research shows that the active HydA1 can be biosynthesized without the maturases HydG and HydE by using a synthetic cluster.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2022)
Article
Chemistry, Multidisciplinary
Batuhan Balci, Roark D. O'Neill, Eric M. Shepard, Adrien Pagnier, Alexander Marlott, Michael T. Mock, William E. Broderick, Joan B. Broderick
Summary: We investigated the maturation of [FeFe]-hydrogenase by using a synthetic complex [Fe-2(& mu;-SH)(2)(CN)(2)(CO)(4)](2-) and the components of glycine cleavage system together with HydF, without the presence of the maturases HydE and HydG. This semisynthetic and fully-defined maturation process offers new insights into the biosynthesis of H-cluster.
CHEMICAL COMMUNICATIONS
(2023)
Review
Chemistry, Multidisciplinary
Julian T. Kleinhaus, Florian Wittkamp, Shanika Yadav, Daniel Siegmund, Ulf-Peter Apfel
Summary: This review provides an overview of developments in [FeFe]-hydrogenase research, focusing on synthetic mimics and their application within the native enzymatic environment.
CHEMICAL SOCIETY REVIEWS
(2021)
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
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)
Correction
Chemistry, Multidisciplinary
Melanie Heghmanns, Andreas Rutz, Yury Kutin, Vera Engelbrecht, Martin Winkler, Thomas Happe, Muege Kasanmascheff
Summary: Correction for the unknown radical signal in the oxygen-resistant [FeFe]-hydrogenase CbA5H.
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, 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.
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, 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
Chemistry, Multidisciplinary
Ashleigh T. Castner, Ben A. Johnson, Seth M. Cohen, Sascha Ott
Summary: This study focuses on the preparation and characterization of a redox-active PCN-700-based MOF that mimics the [FeFe] hydrogenase enzyme, revealing similarities and limitations in the MOF-enzyme analogy. The dual-functionalized MOF shows nonideal interactions between linkers and restricted mobility of charge-compensating redox-inactive counterions upon successive charging, leading to absent expected redox features in cyclic voltammetry. These nonlinear effects may play an important role in MOFs for catalytic applications.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(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, 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
Jesse L. Ruzicka, Lauren M. Pellows, Hayden Kallas, Katherine E. Shulenberger, Oleg A. Zadvornyy, Bryant Chica, Katherine A. Brown, John W. Peters, Paul W. King, Lance C. Seefeldt, Gordana Dukovic
Summary: This study explores the light-driven catalysis of N2 reduction by combining CdS nanorods with the MoFe protein of nitrogenase. The efficiency of electron transfer and product formation is limited by the binding of NRs to MoFe protein and the competitiveness of electron transfer. Characterizing ET kinetics for CdS NRs of varying dimensions reveals a maximum NR diameter for driving the MoFe protein photochemically, providing insights for designing systems with increased control of N2 reduction catalyzed by the MoFe protein.
JOURNAL OF PHYSICAL CHEMISTRY C
(2022)
Article
Chemistry, Multidisciplinary
Bryant Chica, Jesse Ruzicka, Lauren M. Pellows, Hayden Kallas, Effie Kisgeropoulos, Gregory E. Vansuch, David W. Mulder, Katherine A. Brown, Drazenka Svedruzic, John W. Peters, Gordana Dukovic, Lance C. Seefeldt, Paul W. King
Summary: The [8Fe-7S] P-cluster of nitrogenase MoFe protein plays a role in electron transfer during the catalytic production of ammonia. By using photochemical reduction and EPR analysis, it was found that the formation of P+intermediates during electron transfer can be trapped and studied. The results demonstrate the coupling between spin-state transitions and changes in P-cluster oxidation state during electron transfer in MoFe protein.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2022)
Article
Multidisciplinary Sciences
Courtney E. Wise, Anastasia E. Ledinina, David W. Mulder, Katherine J. Chou, John W. Peters, Paul W. King, Carolyn E. Lubner
Summary: Electron bifurcation is an energy-conserving process widely utilized in biochemistry, which generates high-energy products from substrates with lower reducing potential. The energetic challenge of the first bifurcation event, with a thermodynamically uphill step, is resolved by elucidating the unusually low two-electron potential of the bifurcating flavin.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2022)
Article
Microbiology
Lindsay C. Sidak-Loftis, Kristin L. Rosche, Natasha Pence, Jessica K. Ujczo, Joanna Hurtado, Elis A. Fisk, Alan G. Goodman, Susan M. Noh, John W. Peters, Dana K. Shaw
Summary: The study discovers a novel linkage between the unfolded-protein response (UPR) and the immune deficiency (IMD) pathway in arthropods, explaining how the IMD pathway can be activated in ticks and restrict the transmission of pathogens.
Meeting Abstract
Biochemistry & Molecular Biology
Courtney E. Wise, Anastasia E. Ledinina, David W. Mulder, John W. Peters, Paul W. King, Carolyn E. Lubner
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
(2022)
Correction
Microbiology
Lindsay C. Sidak-Loftis, Kristin L. Rosche, Natasha Pence, Jessica K. Ujczo, Joanna Hurtado, Elis A. Fisk, Alan G. Goodman, Susan M. Noh, John W. Peters, Dana K. Shaw
Review
Biotechnology & Applied Microbiology
Alexander B. Alleman, John W. Peters
Summary: The availability of fixed nitrogen is a limiting factor in ecosystem productivity, but diazotrophs can convert atmospheric dinitrogen to ammonia to overcome this limitation. Diazotrophs are diverse bacteria and archaea that utilize various metabolisms to generate low potential reducing equivalents for the nitrogenase enzyme. Understanding the electron transport systems in diazotrophs is essential for future engineering strategies to enhance biological nitrogen fixation in agriculture.
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
(2023)
Article
Chemistry, Multidisciplinary
Gregory E. Vansuch, David W. Mulder, Bryant Chica, Jesse L. Ruzicka, Zhi-Yong Yang, Lauren M. Pellows, Mark A. Willis, Katherine A. Brown, Lance C. Seefeldt, John W. Peters, Gordana Dukovic, Paul W. King
Summary: Experimental evidence shows that the addition of hydrogen is associative with the E-4(2N(2)H) state, thereby revealing a key step in the mechanism of N-2 reduction catalyzed by the enzyme nitrogenase.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Review
Biochemistry & Molecular Biology
Julia S. Martin del Campo, Jack Rigsbee, Marcelo Bueno Batista, Florence Mus, Luis M. Rubio, Oliver Einsle, John W. Peters, Ray Dixon, Dennis R. Dean, Patricia C. Dos Santos
Summary: Understanding the reduction of nitrogen gas to ammonia at ambient conditions has been a longstanding challenge. This knowledge is crucial for transferring biological nitrogen fixation to crops and developing improved synthetic catalysts. Azotobacter vinelandii has emerged as the preferred model organism for studying this process over the past 30 years. This review summarizes the current understanding and places it in historical context.
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
(2022)
Article
Chemistry, Multidisciplinary
Gregory E. Vansuch, David W. Mulder, Bryant Chica, Jesse L. Ruzicka, Zhi-Yong Yang, Lauren M. Pellows, Mark A. Willis, Katherine A. Brown, Lance C. Seefeldt, John W. Peters, Gordana Dukovic, Paul W. King
Summary: Photodriven electron delivery in the frozen state using CdS quantum dots in complex with MoFe protein reveals details of the E-state species and tests the stability of E-4(2N2H). The results establish that the oxidative addition of H-2 to the E-4(2N2H) state follows an associative reaction mechanism.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Chemistry, Multidisciplinary
Sharon L. Smolinski, Carolyn E. Lubner, Zhanjun Guo, Jacob H. Artz, Katherine A. Brown, David W. Mulder, Paul W. King
Summary: The ability of cyanobacteria to adapt to changing photon flux and nutrient availability conditions is due to the controlled management of reducing power. In the absence of ORR1, the photochemical activity of PSI is modulated in coordination with the decrease in electron demand.
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.