Spectroscopic and Electrochemical Characterization of the [NiFeSe] Hydrogenase fromDesulfovibrio vulgarisMiyazaki F: Reversible Redox Behavior and Interactions between Electron Transfer Centers

A Metal–Metal Bond in the Light-Induced State of [NiFe] Hydrogenases with Relevance to Hydrogen Evolution

(2013) Mario Kampa et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Observation of the FeCN and FeCO Vibrations in the Active Site of [NiFe] Hydrogenase by Nuclear Resonance Vibrational Spectroscopy

(2012) Saeed Kamali et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Reversible Electrocatalytic Production and Oxidation of Hydrogen at Low Overpotentials by a Functional Hydrogenase Mimic

(2012) Stuart E. Smith et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Novel H2-oxidizing [NiFeSe]hydrogenase from Desulfovibrio vulgaris Miyazaki F

(2012) Kyoshiro Nonaka et al.   JOURNAL OF BIOSCIENCE AND BIOENGINEERING

X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli

(2012) A. Volbeda et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Electronic structure of the unique [4Fe-3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mossbauer and EPR spectroscopy

(2012) M.-E. Pandelia et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Detergent selection for enhanced extraction of membrane proteins

(2012) Buenafe T. Arachea et al.   PROTEIN EXPRESSION AND PURIFICATION

Spectroscopic characterization of the key catalytic intermediate Ni–C in the O2-tolerant [NiFe] hydrogenase I from Aquifex aeolicus: evidence of a weakly bound hydride

(2011) Maria-Eirini Pandelia et al.   CHEMICAL COMMUNICATIONS

Sulfoxygenation of Active Site Models of [NiFe] and [FeFe] Hydrogenases - A Commentary on Possible Chemical Models of Hydrogenase Enzyme Oxygen Sensitivity

(2011) Marcetta Y. Darensbourg et al.   EUROPEAN JOURNAL OF INORGANIC CHEMISTRY

Nickel-Iron-Selenium Hydrogenases - An Overview

(2011) Carla S. A. Baltazar et al.   EUROPEAN JOURNAL OF INORGANIC CHEMISTRY

Excited-State Intermolecular Proton Transfer of Firefly Luciferin IV. Temperature and pH Dependence

(2011) Yuval Erez et al.   JOURNAL OF PHYSICAL CHEMISTRY A

Oxygen-Tolerant [NiFe]-Hydrogenases: The Individual and Collective Importance of Supernumerary Cysteines at the Proximal Fe-S Cluster

(2011) Michael J. Lukey et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The [NiFe]-Hydrogenase of the CyanobacteriumSynechocystissp. PCC 6803 Works Bidirectionally with a Bias to H2Production

(2011) Chelsea L. McIntosh et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Fast and efficient molecular electrocatalysts for H2 production: Using hydrogenase enzymes as guides

(2011) Jenny Y. Yang et al.   MRS BULLETIN

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

(2011) Johannes Fritsch et al.   NATURE

Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase

(2011) Yasuhito Shomura et al.   NATURE

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase

(2011) Tobias Goris et al.   Nature Chemical Biology

Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus

(2011) M.-E. Pandelia et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

A Synthetic Nickel Electrocatalyst with a Turnover Frequency Above 100,000 s-1 for H2 Production

(2011) M. L. Helm et al.   SCIENCE

Probing the Active Site of an O2-Tolerant NAD+-Reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 by In Situ EPR and FTIR Spectroscopy

(2010) Marius Horch et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Enzymatic Anodes for Hydrogen Fuel Cells based on Covalent Attachment of Ni-Fe Hydrogenases and Direct Electron Transfer to SAM-Modified Gold Electrodes

(2010) Olaf Rüdiger et al.   ELECTROANALYSIS

Thiolate-Bridged Iron-Nickel Models for the Active Site of [NiFe] Hydrogenase

(2010) Yasuhiro Ohki et al.   EUROPEAN JOURNAL OF INORGANIC CHEMISTRY

Electron flow through proteins

(2009) Harry B. Gray et al.   CHEMICAL PHYSICS LETTERS

Structural and Functional Analogues of the Active Sites of the [Fe]-, [NiFe]-, and [FeFe]-Hydrogenases†

(2009) Cédric Tard et al.   CHEMICAL REVIEWS

[NiFe] hydrogenases: structural and spectroscopic studies of the reaction mechanism

(2009) Hideaki Ogata et al.   DALTON TRANSACTIONS

The Three-Dimensional Structure of [NiFeSe] Hydrogenase from Desulfovibrio vulgaris Hildenborough: A Hydrogenase without a Bridging Ligand in the Active Site in Its Oxidised, “as-Isolated” State

(2009) Marta C. Marques et al.   JOURNAL OF MOLECULAR BIOLOGY

Nickel−Iron Dithiolato Hydrides Relevant to the [NiFe]-Hydrogenase Active Site

(2009) Bryan E. Barton et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Visible Light-Driven H2Production by Hydrogenases Attached to Dye-Sensitized TiO2Nanoparticles

(2009) Erwin Reisner et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology

(2008) Fraser A. Armstrong et al.   CHEMICAL SOCIETY REVIEWS

Solar water-splitting into H2 and O2: design principles of photosystem II and hydrogenases

(2008) Wolfgang Lubitz et al.   Energy & Environmental Science

FTIR spectroelectrochemical characterization of the Ni–Fe–Se hydrogenase from Desulfovibrio vulgaris Hildenborough

(2008) Antonio L. De Lacey et al.   JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY

The Difference a Se Makes? Oxygen-Tolerant Hydrogen Production by the [NiFeSe]-Hydrogenase fromDesulfomicrobium baculatum

(2008) Alison Parkin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site

(2008) S. Shima et al.   SCIENCE

Modelling NiFe hydrogenases: nickel-based electrocatalysts for hydrogen production

(2007) Sigolène Canaguier et al.   DALTON TRANSACTIONS