4.4 Review

A personal account on 25 years of scientific literature on [FeFe]-hydrogenase

Related references

Note: Only part of the references are listed.
Article Chemistry, Multidisciplinary

Molecular Basis of the Electron Bifurcation Mechanism in the [FeFe]- Hydrogenase Complex HydABC

Alexander. Katsyv et al.

Summary: Electron bifurcation is a fundamental energy coupling mechanism used by microorganisms in anoxic conditions to reduce CO2 using hydrogen. The enzyme responsible for these reactions, HydABC, uses a single flavin mononucleotide (FMN) cofactor to transfer electrons to NAD(P)+ and low-potential ferredoxins (Fd), and switches between NAD(P)+ reduction and Fd reduction modes. Understanding the mechanistic principles of electron-bifurcating hydrogenases can provide insight into energy conversion processes in microorganisms.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2023)

Article Chemistry, Multidisciplinary

Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway

Jifu Duan et al.

Summary: In this study, the crystal structures of CN--treated [FeFe]-hydrogenase CpI from Clostridium pasteurianum were obtained, revealing that extrinsic CN- binds to the open coordination site of the cofactor. The binding of CN- leads to conformational changes in conserved residues within the proton transfer pathway, potentially facilitating efficient proton transfer. This observation provides important insights into the mechanism of CN- inhibition and proton transfer in hydrogenases.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2023)

Article Biochemistry & Molecular Biology

Accumulation and Pulse Electron Paramagnetic Resonance Spectroscopic Investigation of the 4-Oxidobenzyl Radical Generated in the Radical S-Adenosyl-L-methionine Enzyme HydG

Guodong Rao et al.

Summary: The concentration of trapped 4-OB center dot in reactions using HydG variants is significantly increased, allowing for detailed characterization using high-field EPR and electron nuclear double resonance spectroscopy. The results indicate that the electronic structure of 4-OB center dot is best fit for the deprotonated radical anion configuration.

BIOCHEMISTRY (2022)

Article Chemistry, Multidisciplinary

Organometallic Fe2(μ-SH)2(CO)4(CN)2 Cluster Allows the Biosynthesis of the [FeFe]-Hydrogenase with Only the HydF Maturase

Yu Zhang et al.

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)

Review Microbiology

Microbial oxidation of atmospheric trace gases

Chris Greening et al.

Summary: The oxidation of atmospheric trace gases by microorganisms is an important source of energy for sustaining life. Microbes use specific enzymes to oxidize gases such as hydrogen, carbon monoxide, and methane for aerobic respiration and carbon fixation. This process plays crucial roles in enhancing biodiversity, ecosystem resilience, and mitigating anthropogenic emissions.

NATURE REVIEWS MICROBIOLOGY (2022)

Review Chemistry, Multidisciplinary

Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase

Sven T. Stripp et al.

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.

CHEMICAL REVIEWS (2022)

Article Chemistry, Inorganic & Nuclear

Trapping an Oxidized and Protonated Intermediate of the [FeFe]-Hydrogenase Cofactor under Mildly Reducing Conditions

Moritz Senger et al.

Summary: The H-cluster is the catalytic cofactor of [FeFe]-hydrogenase, and its diiron site can be studied by IR spectroscopy. Previous research identified an oxidized and protonated H-cluster species, HoxH, which is influenced by pH and the presence of external reductants. Recent studies suggest that the accumulation of HoxH is not dependent on specific reductants, but rather on the protonation state and deprotonation ability of the H-cluster.

INORGANIC CHEMISTRY (2022)

Review Chemistry, Multidisciplinary

[FeFe]-Hydrogenase In Vitro Maturation

Adrien Pagnier et al.

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 Biology

Structural insight on the mechanism of an electron-bifurcating [FeFe] hydrogenase

Chris Furlan et al.

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.

ELIFE (2022)

Article Chemistry, Physical

Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment

Solomon L. D. Wrathall et al.

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

The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal

Melanie Heghmanns et al.

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.

CHEMICAL SCIENCE (2022)

Review Chemistry, Multidisciplinary

Proton Transfer Mechanisms in Bimetallic Hydrogenases

Hulin Tai et al.

Summary: Hydrogenases are metalloenzymes capable of efficiently catalyzing proton reduction and hydrogen oxidation. This Account discusses the use of photochemistry and infrared spectroscopy to study the dynamic hydrogen-bonding changes in [NiFe]- and [FeFe]-hydrogenases, revealing distinct structures and functions in these systems.

ACCOUNTS OF CHEMICAL RESEARCH (2021)

Review Chemistry, Inorganic & Nuclear

The catalytic cycle of [FeFe] hydrogenase: A tale of two sites

James A. Birrell et al.

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 Multidisciplinary Sciences

A safety cap protects hydrogenase from oxygen attack

Martin Winkler et al.

Summary: The protein morphing mechanism of [FeFe]-hydrogenase CbA5H controls the reversible transition between catalytic and inactive states, with a conserved cysteine residue protecting the active site from oxygen by acting as a safety cap. This protection mechanism is regulated by three non-conserved amino acids located approximately 13 angstrom away from the active site, demonstrating remote control of the first coordination sphere chemistry of the H-cluster.

NATURE COMMUNICATIONS (2021)

Article Chemistry, Physical

Mechanism of Hydrogen Sulfide-Dependent Inhibition of FeFe Hydrogenase

Christina Felbek et al.

Summary: The study investigates the inhibitory mechanism of hydrogen sulfide on FeFe hydrogenase through a combination of various experimental and theoretical methods, revealing the underlying mechanisms and providing insights into the oxidation and reduction of the enzyme. Additionally, it was observed that the inhibition by sulfide may lead to irreversible inactivation of the hydrogenase.

ACS CATALYSIS (2021)

Review Biochemistry & Molecular Biology

Insights into metalloproteins and metallodrugs from electron paramagnetic resonance spectroscopy

Jana Eisermann et al.

Summary: Metal ions play vital roles in biological processes, and studying metalloproteins and metallodrugs helps in advancing the understanding of metal-based structures and functions.

CURRENT OPINION IN CHEMICAL BIOLOGY (2021)

Review Chemistry, Multidisciplinary

Reversible catalysis

Vincent Fourmond et al.

Summary: Understanding the relationship between reaction rate and thermodynamic driving force is crucial for developing efficient catalysts. This Perspective discusses reversible catalysis, which allows reactions to proceed rapidly and efficiently even with slight deviations from equilibrium. The perspective also covers electrochemical investigations of redox reactions, biological energy transduction, and mean-field kinetic modeling of surface catalysts, molecular catalysts, and molecular machines.

NATURE REVIEWS CHEMISTRY (2021)

Article Chemistry, Physical

In Situ Infrared Spectroscopy for the Analysis of Gas-processing Metalloenzymes

Sven T. Stripp

Summary: Earth-abundant transition metals play essential roles in cellular gas metabolism, forming gas-processing metalloenzymes that catalyze redox reactions. Biophysicists use techniques like Fourier-transform infrared spectroscopy to study the reaction principles of GPMs. Infrared spectroscopy provides information on catalytic cofactors, amino acid residues, and protein structural changes.

ACS CATALYSIS (2021)

Article Chemistry, Multidisciplinary

The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase

Philip A. Ash et al.

Summary: Controlled formation of catalytically-relevant states within crystals of complex metalloenzymes is a significant challenge, but electrochemical control over single crystals can stabilize specific states for further study and extend mechanistic understanding of proton transfer.

CHEMICAL SCIENCE (2021)

Article Chemistry, Inorganic & Nuclear

Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site

Simone Morra et al.

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

Site-selective protonation of the one-electron reduced cofactor in [FeFe]-hydrogenase

Konstantin Laun et al.

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

[FeFe]-Hydrogenases: maturation and reactivity of enzymatic systems and overview of biomimetic models

Julian T. Kleinhaus et al.

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, Multidisciplinary

Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates

James A. Birrell et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2020)

Article Chemistry, Multidisciplinary

Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases

Jacob H. Artz et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2020)

Article Chemistry, Multidisciplinary

Shedding Light on Proton and Electron Dynamics in [FeFe] Hydrogenases

Christian Lorent et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2020)

Review Chemistry, Multidisciplinary

Methanogenesis involves direct hydride transfer from H2 to an organic substrate

Gangfeng Huang et al.

NATURE REVIEWS CHEMISTRY (2020)

Article Chemistry, Physical

Spin Polarization Reveals the Coordination Geometry of the [FeFe] Hydrogenase Active Site in Its CO-Inhibited State

Edward Reijerse et al.

JOURNAL OF PHYSICAL CHEMISTRY LETTERS (2020)

Article Chemistry, Multidisciplinary

Radical SAM Enzyme HydE Generates Adenosylated Fe(I) Intermediates En Route to the [FeFe]-Hydrogenase Catalytic H-Cluster

Lizhi Tao et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2020)

Article Chemistry, Multidisciplinary

Caught in the Hinact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2-stable State of [FeFe] Hydrogenase

Patricia Rodriguez-Macia et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2020)

Article Biochemistry & Molecular Biology

[FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy

Brigitta Nemeth et al.

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY (2020)

Article Chemistry, Physical

Double-hybrid density functional theory for g-tensor calculations using gauge including atomic orbitals

V. A. Tran et al.

JOURNAL OF CHEMICAL PHYSICS (2020)

Article Chemistry, Multidisciplinary

Investigation of the Unusual Ability of the [FeFe] Hydrogenase from Clostridium beijerinckii to Access an O2-Protected State

Patrick S. Corrigan et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2020)

Article Multidisciplinary Sciences

The roles of long-range proton-coupled electron transfer in the directionality and efficiency of [FeFe]-hydrogenases

Oliver Lampret et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2020)

Article Chemistry, Physical

The Laser-Induced Potential Jump: A Method for Rapid Electron Injection into Oxidoreductase Enzymes

Monica L. K. Sanchez et al.

JOURNAL OF PHYSICAL CHEMISTRY B (2020)

Article Biochemical Research Methods

Towards cryogenic neutron crystallography on the reduced form of [NiFe]-hydrogenase

Takeshi Hiromoto et al.

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2020)

Article Chemistry, Inorganic & Nuclear

Temperature Dependence of Structural Dynamics at the Catalytic Cofactor of [FeFe]-hydrogenase

Sven T. Stripp et al.

INORGANIC CHEMISTRY (2020)

Article Chemistry, Physical

Insight into the Redox Behavior of the [4Fe-4S] Subcluster in [FeFe] Hydrogenases

Patricia Rodriguez-Macia et al.

ACS CATALYSIS (2020)

Article Chemistry, Multidisciplinary

Cysteine SH and Glutamate COOH Contributions to [NiFe] Hydrogenase Proton Transfer Revealed by Highly Sensitive FTIR Spectroscopy

Hulin Tai et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2019)

Article Multidisciplinary Sciences

The final steps of [FeFe]-hydrogenase maturation

Oliver Lampret et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2019)

Article Chemistry, Multidisciplinary

Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-Resolved Infrared Spectroscopy

Monica L. K. Sanchez et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2019)

Article Multidisciplinary Sciences

The binuclear cluster of [FeFe] hydrogenase is formed with sulfur donated by cysteine of an [Fe(Cys)(CO)2(CN)] organometallic precursor

Guodong Rao et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2019)

Article Chemistry, Multidisciplinary

Loss of Specific Active-Site Iron Atoms in Oxygen-Exposed [FeFe]-Hydrogenase Determined by Detailed X-ray Structure Analyses

Julian Esselborn et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2019)

Article Chemistry, Multidisciplinary

How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer

Moritz Senger et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2019)

Review Chemistry, Multidisciplinary

The Molecular Proceedings of Biological Hydrogen Turnover

Michael Haumann et al.

ACCOUNTS OF CHEMICAL RESEARCH (2018)

Article Chemistry, Multidisciplinary

A [RuRu] Analogue of an [FeFe]-Hydrogenase Traps the Key Hydride Intermediate of the Catalytic Cycle

Constanze Sommer et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2018)

Article Biochemistry & Molecular Biology

Hydrogen and oxygen trapping at the H-cluster of [FeFe]-hydrogenase revealed by site-selective spectroscopy and QM/MM calculations

Stefan Mebs et al.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2018)

Review Biochemistry & Molecular Biology

Sulphur-containing Amino Acids: Protective Role Against Free Radicals and Heavy Metals

Mirjana B. Colovic et al.

CURRENT MEDICINAL CHEMISTRY (2018)

Review Biochemistry & Molecular Biology

Resonance Raman spectroscopy of Fe-S proteins and their redox properties

Smilja Todorovic et al.

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY (2018)

Review Biochemistry & Molecular Biology

EPR spectroscopy of complex biological iron-sulfur systems

Wilfred R. Hagen

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY (2018)

Article Chemistry, Multidisciplinary

Direct Detection of the Terminal Hydride Intermediate in [FeFe] Hydrogenase by NMR Spectroscopy

Sigrun Rumpel et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2018)

Article Chemistry, Multidisciplinary

Interaction of the H-Cluster of FeFe Hydrogenase with Halides

Melisa del Barrio et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2018)

Article Chemistry, Multidisciplinary

Unique Spectroscopic Properties of the H-Cluster in a Putative Sensory [FeFe] Hydrogenase

Nipa Chongdar et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2018)

Article Chemistry, Multidisciplinary

Sulfide Protects [FeFe] Hydrogenases From O2

Patricia Rodriguez-Macia et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2018)

Article Multidisciplinary Sciences

Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases

Jifu Duan et al.

NATURE COMMUNICATIONS (2018)

Article Chemistry, Multidisciplinary

Identification of a Catalytic Iron-Hydride at the H-Cluster of [FeFe]-Hydrogenase

David W. Mulder et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2017)

Article Chemistry, Multidisciplinary

Reduction Potentials of [FeFe]-Hydrogenase Accessory Iron-Sulfur Clusters Provide Insights into the Energetics of Proton Reduction Catalysis

Jacob H. Artz et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2017)

Article Chemistry, Multidisciplinary

Intercluster Redox Coupling Influences Protonation at the H-cluster in [FeFe] Hydrogenases

Patricia Rodriguez-Macia et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2017)

Article Chemistry, Multidisciplinary

Interplay between CN- Ligands and the Secondary Coordination Sphere of the H-Cluster in [FeFe]-Hydrogenases

Oliver Lampret et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2017)

Article Chemistry, Multidisciplinary

Proton Coupled Electronic Rearrangement within the H-Cluster as an Essential Step in the Catalytic Cycle of [FeFe] Hydrogenases

Constanze Sommer et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2017)

Article Chemistry, Multidisciplinary

Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy

Edward J. Reijerse et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2017)

Article Multidisciplinary Sciences

Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases

Martin Winkler et al.

NATURE COMMUNICATIONS (2017)

Article Chemistry, Physical

Pre-Steady-State Kinetics of Catalytic Intermediates of an [FeFe]-Hydrogenase

Brandon L. Greene et al.

ACS CATALYSIS (2017)

Article Chemistry, Inorganic & Nuclear

Chalcogenide substitution in the [2Fe] cluster of [FeFe]-hydrogenases conserves high enzymatic activity

L. Kertess et al.

DALTON TRANSACTIONS (2017)

Article Spectroscopy

Quantum Chemistry and EPR Parameters

Frank Neese

EMAGRES (2017)

Review Chemistry, Multidisciplinary

Guiding Principles of Hydrogenase Catalysis Instigated and Clarified by Protein Film Electrochemistry

Fraser A. Armstrong et al.

ACCOUNTS OF CHEMICAL RESEARCH (2016)

Article Chemistry, Multidisciplinary

[FeFe]-Hydrogenase with Chalcogenide Substitutions at the H-Cluster Maintains Full H2 Evolution Activity

Jens Noth et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2016)

Article Chemistry, Multidisciplinary

Artificial Maturation of the Highly Active Heterodimeric [FeFe] Hydrogenase from Desulfovibrio desulfuricans ATCC 7757

James A. Birrell et al.

ISRAEL JOURNAL OF CHEMISTRY (2016)

Article Multidisciplinary Sciences

Stepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamics

Moritz Senger et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2016)

Article Chemistry, Multidisciplinary

Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution

S. Katz et al.

CHEMICAL SCIENCE (2016)

Article Chemistry, Multidisciplinary

A structural view of synthetic cofactor integration into [FeFe]-hydrogenases

J. Esselborn et al.

CHEMICAL SCIENCE (2016)

Article Multidisciplinary Sciences

HydDB: A web tool for hydrogenase classification and analysis

Dan Sondergaard et al.

SCIENTIFIC REPORTS (2016)

Article Biochemistry & Molecular Biology

Hybrid [FeFe]-Hydrogenases with Modified Active Sites Show Remarkable Residual Enzymatic Activity

Judith F. Siebel et al.

BIOCHEMISTRY (2015)

Article Chemistry, Multidisciplinary

[FeFe]-Hydrogenase Oxygen Inactivation Is Initiated at the H Cluster 2Fe Subcluster

Kevin D. Swanson et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2015)

Article Chemistry, Multidisciplinary

Spectroscopic Characterization of the Bridging Amine in the Active Site of [FeFe] Hydrogenase Using lsotopologues of the H-Cluster

Agnieszka Adamska-Venkatesh et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2015)

Article Chemistry, Multidisciplinary

Spectroscopic Investigations of [FeFe] Hydrogenase Maturated with [57Fe2(adt)(CN)2(CO)4]2-

Ryan Gilbert-Wilson et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2015)

Article Chemistry, Physical

Artificially maturated [FeFe] hydrogenase from Chlamydomonas reinhardtii: a HYSCORE and ENDOR study of a non-natural H-cluster

Agnieszka Adamska-Venkatesh et al.

PHYSICAL CHEMISTRY CHEMICAL PHYSICS (2015)

Article Chemistry, Applied

EPR Spectroscopic Studies of [FeFe]-Hydrogenase Maturation

Daniel L. M. Suess et al.

TOPICS IN CATALYSIS (2015)

Article Multidisciplinary Sciences

Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy

Hideaki Ogata et al.

NATURE COMMUNICATIONS (2015)

Review Crystallography

Protein crystallography from the perspective of technology developments

Xiao-Dong Su et al.

CRYSTALLOGRAPHY REVIEWS (2015)

Review Chemistry, Multidisciplinary

Hydrogenases

Wolfgang Lubitz et al.

CHEMICAL REVIEWS (2014)

Article Chemistry, Inorganic & Nuclear

Hydride Binding to the Active Site of [FeFe]-Hydrogenase

Petko Chernev et al.

INORGANIC CHEMISTRY (2014)

Article Chemistry, Multidisciplinary

The Cyanide Ligands of [FeFe] Hydrogenase: Pulse EPR Studies of 13C and 15N-Labeled H-Cluster

William K. Myers et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2014)

Article Chemistry, Multidisciplinary

New Redox States Observed in [FeFe] Hydrogenases Reveal Redox Coupling Within the H-Cluster

Agnieszka Adamska-Venkatesh et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2014)

Article Chemistry, Multidisciplinary

Investigations on the Role of Proton-Coupled Electron Transfer in Hydrogen Activation by [FeFe]-Hydrogenase

David W. Mulder et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2014)

Article Biochemistry & Molecular Biology

Reversible [4Fe-3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase

Stefan Frielingsdorf et al.

NATURE CHEMICAL BIOLOGY (2014)

Review Biochemistry & Molecular Biology

[NiFe] hydrogenases: A common active site for hydrogen metabolism under diverse conditions

Hannah S. Shafaat et al.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2013)

Article Chemistry, Multidisciplinary

EPR and FTIR Analysis of the Mechanism of H2 Activation by [FeFe]-Hydrogenase HydA1 from Chlamydomonas reinhardtii

David W. Mulder et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2013)

Article Multidisciplinary Sciences

Biomimetic assembly and activation of [FeFe]-hydrogenases

G. Berggren et al.

NATURE (2013)

Article Biochemistry & Molecular Biology

Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic

Julian Esselborn et al.

NATURE CHEMICAL BIOLOGY (2013)

Review Biochemistry & Molecular Biology

The hows and whys of aerobic H2 metabolism

Alison Parkin et al.

CURRENT OPINION IN CHEMICAL BIOLOGY (2012)

Article Chemistry, Inorganic & Nuclear

Unraveling the Electronic Properties of the Photoinduced States of the H-Cluster in the [FeFe] Hydrogenase from D. desulfuricans

Alexey Silakov et al.

EUROPEAN JOURNAL OF INORGANIC CHEMISTRY (2011)

Article Multidisciplinary Sciences

The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre

Johannes Fritsch et al.

NATURE (2011)

Review Chemistry, Multidisciplinary

Multifrequency Pulsed Electron Paramagnetic Resonance on Metalloproteins

Sevdalina Lyubenova et al.

ACCOUNTS OF CHEMICAL RESEARCH (2010)

Review Biochemistry & Molecular Biology

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H-2 Storage

Rudolf K. Thauer et al.

ANNUAL REVIEW OF BIOCHEMISTRY, VOL 79 (2010)

Article Multidisciplinary Sciences

Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydAΔEFG

David W. Mulder et al.

NATURE (2010)

Review Microbiology

Nitrogen Fixation and Hydrogen Metabolism in Cyanobacteria

Hermann Bothe et al.

MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS (2010)

Review Chemistry, Multidisciplinary

2D-IR spectroscopy: ultrafast insights into biomolecule structure and function

Neil T. Hunt

CHEMICAL SOCIETY REVIEWS (2009)

Review Chemistry, Inorganic & Nuclear

How algae produce hydrogen-news from the photosynthetic hydrogenase

Sven T. Stripp et al.

DALTON TRANSACTIONS (2009)

Article Multidisciplinary Sciences

How oxygen attacks [FeFe] hydrogenases from photosynthetic organisms

Sven T. Stripp et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)

Article Chemistry, Multidisciplinary

Synthetic Support of De Novo Design: Sterically Bulky [FeFe]-Hydrogenase Models

Michael L. Singleton et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2008)

Article Biochemistry & Molecular Biology

Isolation and first EPR characterization of the [FeFe]-hydrogenases from green algae

Christina Kamp et al.

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2008)

Article Chemistry, Physical

Optimized over-expression of [FeFe] hydrogenases with high specific activity in Clostridium acetobutylicum

Gregory von Abendroth et al.

INTERNATIONAL JOURNAL OF HYDROGEN ENERGY (2008)

Correction Multidisciplinary Sciences

A natural choice for activating hydrogen (vol 321, pg 498, 2008)

F. A. Armstrong et al.

SCIENCE (2008)

Article Multidisciplinary Sciences

The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site

Seigo Shima et al.

SCIENCE (2008)

Review Chemistry, Multidisciplinary

Occurrence, classification, and biological function of hydrogenases: An overview

Paulette M. Vignais et al.

CHEMICAL REVIEWS (2007)

Review Chemistry, Multidisciplinary

Investigating and exploiting the electrocatalytic properties of hydrogenases

Kylie A. Vincent et al.

CHEMICAL REVIEWS (2007)

Review Chemistry, Multidisciplinary

[NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques

Wolfgang Lubitz et al.

CHEMICAL REVIEWS (2007)

Article Chemistry, Multidisciplinary

The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans:: A Q-band 57Fe-ENDOR and HYSCORE study

Alexey Silakov et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2007)

Review Biochemistry & Molecular Biology

Infrared spectroscopy of proteins

Andreas Barth

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2007)

Article Biochemistry & Molecular Biology

Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase

MC Posewitz et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2004)

Review Plant Sciences

Trails of green alga hydrogen research - from Hans Gaffron to new frontiers

A Melis et al.

PHOTOSYNTHESIS RESEARCH (2004)

Article Biochemistry & Molecular Biology

Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii

T Happe et al.

EUROPEAN JOURNAL OF BIOCHEMISTRY (2002)

Article Chemistry, Multidisciplinary

Mossbauer characterization of the iron-sulfur clusters in Desulfovibrio vulgaris hydrogenase

AS Pereira et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2001)

Article Chemistry, Physical

Hydrogen production by biological processes: a survey of literature

D Das et al.

INTERNATIONAL JOURNAL OF HYDROGEN ENERGY (2001)

Article Chemistry, Multidisciplinary

FTIR characterization of the active site of the Fe-hydrogenase from Desulfovibrio desulfuricans

AL De Lacey et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2000)

Article Biochemistry & Molecular Biology

Reversible carbon monoxide binding and inhibition at the active site of the Fe-only hydrogenase

B Bennett et al.

BIOCHEMISTRY (2000)

Article Chemistry, Multidisciplinary

Photochemistry at the active site of the carbon monoxide inhibited form of the iron-only hydrogenase (CpI)

BJ Lemon et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2000)

Article Chemistry, Multidisciplinary

Reversible Glutamate Coordination to High-Valent Nickel Protects the Active Site of a [NiFe] Hydrogenase from Oxygen

Catharina J. Kulka-Peschke et al.

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