Hydrogenases.

[1]  T. Soares,et al.  Single-Amino Acid Modifications Reveal Additional Controls on the Proton Pathway of [FeFe]-Hydrogenase. , 2016, Biochemistry.

[2]  A. Schmidt,et al.  Krypton Derivatization of an O2 -Tolerant Membrane-Bound [NiFe] Hydrogenase Reveals a Hydrophobic Tunnel Network for Gas Transport. , 2016, Angewandte Chemie.

[3]  O. Lenz,et al.  Structure of an Actinobacterial-Type [NiFe]-Hydrogenase Reveals Insight into O2-Tolerant H2 Oxidation. , 2016, Structure.

[4]  S. Shima,et al.  Reconstitution of [Fe]-hydrogenase using model complexes. , 2015, Nature chemistry.

[5]  W. Lubitz,et al.  Structural differences between the active sites of the Ni-A and Ni-B states of the [NiFe] hydrogenase: an approach by quantum chemistry and single crystal ENDOR spectroscopy. , 2015, Physical chemistry chemical physics : PCCP.

[6]  W. Lubitz,et al.  Cofactor composition and function of a H2-sensing regulatory hydrogenase as revealed by Mössbauer and EPR spectroscopy† †Electronic supplementary information (ESI) available: Tables with the simulation parameters and details of the Mössbauer, and EPR spectra (Tables S1–S4). additional EPR and Mössba , 2015, Chemical science.

[7]  W. Lubitz,et al.  Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase , 2015, Nature.

[8]  Dennis R. Dean,et al.  Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage , 2014, Chemical reviews.

[9]  Christopher H. Chang,et al.  Proton transport in Clostridium pasteurianum [FeFe] hydrogenase I: a computational study. , 2014, The journal of physical chemistry. B.

[10]  W. Lubitz,et al.  Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic. , 2013, Nature chemical biology.

[11]  W. Lubitz,et al.  Spectroscopic and Electrochemical Characterization of the [NiFeSe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Reversible Redox Behavior and Interactions between Electron Transfer Centers , 2013, Chembiochem : a European journal of chemical biology.

[12]  A. L. Lacey,et al.  Orientation and Function of a Membrane-Bound Enzyme Monitored by Electrochemical Surface-Enhanced Infrared Absorption Spectroscopy , 2013 .

[13]  Mei Wang,et al.  Reactions of [FeFe]-hydrogenase models involving the formation of hydrides related to proton reduction and hydrogen oxidation. , 2013, Dalton transactions.

[14]  P. Matias,et al.  Redox State-Dependent Changes in the Crystal Structure of [Nifese] Hydrogenase from Desulfovibrio Vulgaris Hildenborough , 2013 .

[15]  A. Volbeda,et al.  Structural foundations for the O2 resistance of Desulfomicrobium baculatum [NiFeSe]-hydrogenase. , 2013, Chemical communications.

[16]  W. Lubitz,et al.  Biomimetic assembly and activation of [FeFe]-hydrogenases , 2013, Nature.

[17]  O. Lenz,et al.  Novel, Oxygen-Insensitive Group 5 [NiFe]-Hydrogenase in Ralstonia eutropha , 2013, Applied and Environmental Microbiology.

[18]  Xile Hu,et al.  [Fe]-hydrogenase and models that contain iron-acyl ligation. , 2013, Chemistry, an Asian journal.

[19]  S. Frielingsdorf,et al.  Resonance Raman spectroscopy as a tool to monitor the active site of hydrogenases. , 2013, Angewandte Chemie.

[20]  J. W. Peters,et al.  EPR and FTIR analysis of the mechanism of H2 activation by [FeFe]-hydrogenase HydA1 from Chlamydomonas reinhardtii. , 2013, Journal of the American Chemical Society.

[21]  F. Neese,et al.  A metal-metal bond in the light-induced state of [NiFe] hydrogenases with relevance to hydrogen evolution. , 2013, Journal of the American Chemical Society.

[22]  W. Myers,et al.  Nuclear resonance vibrational spectroscopy and electron paramagnetic resonance spectroscopy of 57Fe-enriched [FeFe] hydrogenase indicate stepwise assembly of the H-cluster. , 2013, Biochemistry.

[23]  O. Lenz,et al.  Structure, function and biosynthesis of O2-tolerant hydrogenases , 2013, Nature Reviews Microbiology.

[24]  D. Byrne,et al.  Observation of the Fe-CN and Fe-CO vibrations in the active site of [NiFe] hydrogenase by nuclear resonance vibrational spectroscopy. , 2013, Angewandte Chemie.

[25]  W. Lubitz,et al.  Identification and characterization of the "super-reduced" state of the H-cluster in [FeFe] hydrogenase: a new building block for the catalytic cycle? , 2012, Angewandte Chemie.

[26]  C. Léger,et al.  Understanding and tuning the catalytic bias of hydrogenase. , 2012, Journal of the American Chemical Society.

[27]  F. Armstrong,et al.  Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation. , 2012, Journal of the American Chemical Society.

[28]  G. Maróti,et al.  Analyses of the Large Subunit Histidine-Rich Motif Expose an Alternative Proton Transfer Pathway in [NiFe] Hydrogenases , 2012, PloS one.

[29]  Y. Higuchi,et al.  Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase , 2011, Nature.

[30]  C. Spahn,et al.  The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre , 2011, Nature.

[31]  M. Haumann,et al.  O2 Reactions at the Six-iron Active Site (H-cluster) in [FeFe]-Hydrogenase* , 2011, The Journal of Biological Chemistry.

[32]  J. W. Peters,et al.  Mechanism of Proton Transfer in [FeFe]-Hydrogenase from Clostridium pasteurianum* , 2011, The Journal of Biological Chemistry.

[33]  R. Morris Bullock,et al.  A Synthetic Nickel Electrocatalyst with a Turnover Frequency Above 100,000 s−1 for H2 Production , 2011, Science.

[34]  S. Frielingsdorf,et al.  Role of the HoxZ subunit in the electron transfer pathway of the membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha immobilized on electrodes. , 2011, The journal of physical chemistry. B.

[35]  G. Hong,et al.  On understanding proton transfer to the biocatalytic [Fe-Fe](H) sub-cluster in [Fe-Fe]H(2)ases: QM/MM MD simulations. , 2011, Biochimica et biophysica acta.

[36]  V. Fernández,et al.  Oriented immobilization of a membrane-bound hydrogenase onto an electrode for direct electron transfer. , 2011, Langmuir : the ACS journal of surfaces and colloids.

[37]  W. Lubitz,et al.  SEIRA spectroscopy of the electrochemical activation of an immobilized [NiFe] hydrogenase under turnover and non-turnover conditions. , 2011, Angewandte Chemie.

[38]  B. Guigliarelli,et al.  Original design of an oxygen-tolerant [NiFe] hydrogenase: major effect of a valine-to-cysteine mutation near the active site. , 2011, Journal of the American Chemical Society.

[39]  D. Dubois,et al.  Fast and efficient molecular electrocatalysts for H_2 production: Using hydrogenase enzymes as guides , 2011 .

[40]  W. Lubitz,et al.  The crystal structure of the [NiFe] hydrogenase from the photosynthetic bacterium Allochromatium vinosum: characterization of the oxidized enzyme (Ni-A state). , 2010, Journal of molecular biology.

[41]  W. Lubitz,et al.  Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus: enzyme activation, redox intermediates and oxygen tolerance. , 2010, Journal of the American Chemical Society.

[42]  J. W. Peters,et al.  Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydAΔEFG , 2010, Nature.

[43]  W. Lubitz,et al.  Intermediates in the catalytic cycle of [NiFe] hydrogenase: functional spectroscopy of the active site. , 2010, Chemphyschem : a European journal of chemical physics and physical chemistry.

[44]  F. Stellato,et al.  The iron-site structure of [Fe]-hydrogenase and model systems: an X-ray absorption near edge spectroscopy study. , 2010, Dalton transactions.

[45]  P. Matias,et al.  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. , 2010, Journal of molecular biology.

[46]  W. Lubitz,et al.  Comparison of the membrane-bound [NiFe] hydrogenases from R. eutropha H16 and D. vulgaris Miyazaki F in the oxidized ready state by pulsed EPR. , 2010, Physical chemistry chemical physics : PCCP.

[47]  W. Lubitz,et al.  Inhibition of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F by carbon monoxide: an FTIR and EPR spectroscopic study. , 2010, Biochimica et biophysica acta.

[48]  Wolfgang Lubitz,et al.  Spectroelectrochemical study of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F in solution and immobilized on biocompatible gold surfaces. , 2009, The journal of physical chemistry. B.

[49]  W. Lubitz,et al.  FTIR study on the light sensitivity of the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: Ni-C to Ni-L photoconversion, kinetics of proton rebinding and H/D isotope effect. , 2009, Physical chemistry chemical physics : PCCP.

[50]  W. Lubitz,et al.  [NiFe] hydrogenases: structural and spectroscopic studies of the reaction mechanism. , 2009, Dalton transactions.

[51]  S. Shima,et al.  The crystal structure of an [Fe]-hydrogenase-substrate complex reveals the framework for H2 activation. , 2009, Angewandte Chemie.

[52]  Patricia Amara,et al.  Structure–function relationships of anaerobic gas-processing metalloenzymes , 2009, Nature.

[53]  W. Lubitz,et al.  Spectroelectrochemical characterization of the active site of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii. , 2009, Biochemistry.

[54]  B. Wenk,et al.  (14)N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: evidence for a nitrogen in the dithiol bridge. , 2009, Physical chemistry chemical physics : PCCP.

[55]  Xinzheng Yang,et al.  Monoiron hydrogenase catalysis: hydrogen activation with the formation of a dihydrogen, Fe-H(delta-)...H(delta+)-O, bond and methenyl-H4MPT+ triggered hydride transfer. , 2009, Journal of the American Chemical Society.

[56]  C. Pickett,et al.  Structural and functional analogues of the active sites of the [Fe]-, [NiFe]-, and [FeFe]-hydrogenases. , 2009, Chemical reviews.

[57]  O. Lenz,et al.  Spectroscopic Insights into the Oxygen-tolerant Membrane-associated [NiFe] Hydrogenase of Ralstonia eutropha H16* , 2009, The Journal of Biological Chemistry.

[58]  S. Shima,et al.  The crystal structure of C176A mutated [Fe]‐hydrogenase suggests an acyl‐iron ligation in the active site iron complex , 2009, FEBS letters.

[59]  A. L. Lacey,et al.  FTIR spectroelectrochemical characterization of the Ni–Fe–Se hydrogenase from Desulfovibrio vulgaris Hildenborough , 2008, JBIC Journal of Biological Inorganic Chemistry.

[60]  S. Shima,et al.  The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site , 2008, Science.

[61]  Xiaoming Liu,et al.  The iron centre of the cluster-free hydrogenase (Hmd): low-spin Fe(II) or low-spin Fe(0)? , 2008, Chemical communications.

[62]  W. Lubitz,et al.  Solar water-splitting into H2 and O2: design principles of photosystem II and hydrogenases , 2008 .

[63]  F. Armstrong,et al.  Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis. , 2008, Chemical reviews.

[64]  D. Case,et al.  Characterization of the Fe site in iron-sulfur cluster-free hydrogenase (Hmd) and of a model compound via nuclear resonance vibrational spectroscopy (NRVS). , 2008, Inorganic chemistry.

[65]  R. Ely,et al.  Thermotolerant Hydrogenases: Biological Diversity, Properties, and Biotechnological Applications , 2008 .

[66]  Per E M Siegbahn,et al.  Computational studies of [NiFe] and [FeFe] hydrogenases. , 2007, Chemical reviews.

[67]  P. Vignais,et al.  Occurrence, classification, and biological function of hydrogenases: an overview. , 2007, Chemical reviews.

[68]  Yvain Nicolet,et al.  Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. , 2007, Chemical reviews.

[69]  F. Armstrong,et al.  Investigating and exploiting the electrocatalytic properties of hydrogenases. , 2007, Chemical reviews.

[70]  V. Fernández,et al.  Activation and inactivation of hydrogenase function and the catalytic cycle: spectroelectrochemical studies. , 2007, Chemical reviews.

[71]  P. Siegbahn.  Hybrid density functional study of the oxidized states of NiFe-hydrogenase , 2007 .

[72]  A. L. Lacey,et al.  Characterization of the active site of catalytically inactive forms of [NiFe] hydrogenases by density functional theory , 2007, JBIC Journal of Biological Inorganic Chemistry.

[73]  N. Kervarec,et al.  Evidence for the formation of terminal hydrides by protonation of an asymmetric iron hydrogenase active site mimic. , 2007, Inorganic chemistry.

[74]  S. Shima,et al.  The Iron-Sulfur Cluster-free Hydrogenase (Hmd) Is a Metalloenzyme with a Novel Iron Binding Motif* , 2006, Journal of Biological Chemistry.

[75]  C. Vonrhein,et al.  The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase. , 2006, Journal of molecular biology.

[76]  L. De Gioia,et al.  Proton reduction and dihydrogen oxidation on models of the [2Fe]H cluster of [Fe] hydrogenases. A density functional theory investigation. , 2006, Inorganic chemistry.

[77]  H. Ogata,et al.  Redox interaction of cytochrome c3 with [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F. , 2006, Biochemistry.

[78]  H. Ogata,et al.  Activation process of [NiFe] hydrogenase elucidated by high-resolution X-ray analyses: conversion of the ready to the unready state. , 2005, Structure.

[79]  Scott R. Wilson,et al.  Characterization of a diferrous terminal hydride mechanistically relevant to the Fe-only hydrogenases. , 2005, Journal of the American Chemical Society.

[80]  F. Armstrong,et al.  Hydrogen cycling by enzymes: electrocatalysis and implications for future energy technology. , 2005, Dalton transactions.

[81]  M. Fontecave,et al.  Some general principles for designing electrocatalysts with hydrogenase activity , 2005 .

[82]  M. Bruschi,et al.  DFT investigations of models related to the active site of [NiFe] and [Fe] hydrogenases , 2005 .

[83]  V. Belle,et al.  Hyperthermostable and oxygen resistant hydrogenases from a hyperthermophilic bacterium Aquifex aeolicus: Physicochemical properties , 2005 .

[84]  S. Shima,et al.  Mössbauer studies of the iron-sulfur cluster-free hydrogenase: the electronic state of the mononuclear Fe active site. , 2005, Journal of the American Chemical Society.

[85]  O. Lenz,et al.  Oxygen Tolerance of the H2-sensing [NiFe] Hydrogenase from Ralstonia eutropha H16 Is Based on Limited Access of Oxygen to the Active Site* , 2005, Journal of Biological Chemistry.

[86]  F. Armstrong,et al.  [NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates , 2005, Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences.

[87]  F. Armstrong,et al.  Investigating metalloenzyme reactions using electrochemical sweeps and steps: fine control and measurements with reactants ranging from ions to gases. , 2005, Inorganic chemistry.

[88]  F. Neese,et al.  EPR experiments to elucidate the structure of the ready and unready states of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F. , 2005, Biochemical Society transactions.

[89]  F. Armstrong,et al.  Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states. , 2004, Journal of the American Chemical Society.

[90]  S. Shima,et al.  Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy. , 2004, Journal of the American Chemical Society.

[91]  A. L. Lacey,et al.  The activation of the [NiFe]-hydrogenase from Allochromatium vinosum. An infrared spectro-electrochemical study , 2004, JBIC Journal of Biological Inorganic Chemistry.

[92]  S. George,et al.  Hydrogen-induced activation of the [NiFe]-hydrogenase from Allochromatium vinosum as studied by stopped-flow infrared spectroscopy. , 2004, Biochemistry.

[93]  S. George,et al.  Reactions of H2, CO, and O2 with active [NiFe]-hydrogenase from Allochromatium vinosum. A stopped-flow infrared study. , 2004, Biochemistry.

[94]  C. Griesinger,et al.  The cofactor of the iron-sulfur cluster free hydrogenase hmd: structure of the light-inactivation product. , 2004, Angewandte Chemie.

[95]  C. Lancaster,et al.  Characterization of the Menaquinone Reduction Site in the Diheme Cytochrome b Membrane Anchor of Wolinella succinogenes NiFe-hydrogenase* , 2004, Journal of Biological Chemistry.

[96]  W. Lubitz,et al.  Direct detection of a hydrogen ligand in the [NiFe] center of the regulatory H2-sensing hydrogenase from Ralstonia eutropha in its reduced state by HYSCORE and ENDOR spectroscopy. , 2003, Journal of the American Chemical Society.

[97]  C. Pickett,et al.  Chemistry and the hydrogenases. , 2003, Chemical Society reviews.

[98]  L. De Gioia,et al.  Density functional theory investigation of the active site of [Fe]-hydrogenases: effects of redox state and ligand characteristics on structural, electronic, and reactivity properties of complexes related to the [2Fe]H subcluster. , 2003, Inorganic chemistry.

[99]  M. Darensbourg,et al.  Activation of alkenes and H2 by [Fe]-H2ase model complexes. , 2003, Journal of the American Chemical Society.

[100]  W. Lubitz,et al.  Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F. , 2003, Journal of the American Chemical Society.

[101]  N. Yasuoka,et al.  Structural studies of the carbon monoxide complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F: suggestion for the initial activation site for dihydrogen. , 2002, Journal of the American Chemical Society.

[102]  M. Darensbourg,et al.  Catalysis of H(2)/D(2) scrambling and other H/D exchange processes by [Fe]-hydrogenase model complexes. , 2002, Inorganic chemistry.

[103]  Shuhua Li,et al.  IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibriofructosovorans Ni-Fe hydrogenase , 2002, JBIC Journal of Biological Inorganic Chemistry.

[104]  B. Hoffman,et al.  17O ENDOR detection of a solvent-derived Ni-(OH(x))-Fe bridge that is lost upon activation of the hydrogenase from Desulfovibrio gigas. , 2002, Journal of the American Chemical Society.

[105]  J. Meyer,et al.  Classification and phylogeny of hydrogenases. , 2001, FEMS microbiology reviews.

[106]  H. Fan,et al.  A capable bridging ligand for Fe-only hydrogenase: density functional calculations of a low-energy route for heterolytic cleavage and formation of dihydrogen. , 2001, Journal of the American Chemical Society.

[107]  S. Shima,et al.  The metal‐free hydrogenase from methanogenic archaea: evidence for a bound cofactor , 2000, FEBS letters.

[108]  E. Kremmer,et al.  Regulation of the synthesis of H2-forming methylenetetrahydromethanopterin dehydrogenase (Hmd) and of HmdII and HmdIII in Methanothermobacter marburgensis , 2000, Archives of Microbiology.

[109]  S. Albracht,et al.  Structural examination of the nickel site in chromatium vinosum hydrogenase: redox state oscillations and structural changes accompanying reductive activation and CO binding. , 2000, Biochemistry.

[110]  W. Lubitz,et al.  Single crystal EPR studies of the oxidized active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F , 2000, JBIC Journal of Biological Inorganic Chemistry.

[111]  C. Friedrich,et al.  Unusual FTIR and EPR properties of the H2‐activating site of the cytoplasmic NAD‐reducing hydrogenase from Ralstonia eutropha , 2000, FEBS letters.

[112]  Christopher C. Moser,et al.  Natural engineering principles of electron tunnelling in biological oxidation–reduction , 1999, Nature.

[113]  B. J. Lemon,et al.  Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum. , 1999, Biochemistry.

[114]  E. Münck,et al.  Electronic Structure of the H Cluster in [Fe]-Hydrogenases , 1999 .

[115]  H. Heering,et al.  Catalytic electron transport in Chromatium vinosum [NiFe]-hydrogenase: application of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H+/H2 value. , 1999, Biochemistry.

[116]  X Vernede,et al.  The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. , 1999, Structure.

[117]  J. Fontecilla-Camps,et al.  Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. , 1999, Structure.

[118]  B J Lemon,et al.  X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. , 1998, Science.

[119]  W. Hagen,et al.  A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases. , 1998, European journal of biochemistry.

[120]  N. Yasuoka,et al.  Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis. , 1997, Structure.

[121]  M. Field,et al.  Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics , 1997, Nature Structural Biology.

[122]  A. Pierik,et al.  Biological activition of hydrogen , 1997, Nature.

[123]  A. L. Lacey,et al.  Structure of the [Nife] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands , 1996 .

[124]  B. Guigliarelli,et al.  Spin-spin interactions between the Ni site and the [4Fe-4S] centers as a probe of light-induced structural changes in active Desulfovibrio gigas hydrogenase. , 1996, Biochemistry.

[125]  R. A. Scott,et al.  Structure of the Ni sites in hydrogenases by X-ray absorption spectroscopy. Species variation and the effects of redox poise , 1996 .

[126]  B. Burgess,et al.  Mechanism of Molybdenum Nitrogenase. , 1996, Chemical reviews.

[127]  N. Yasuoka,et al.  Single crystal EPR study of the Ni center of NiFe hydrogenase , 1996 .

[128]  R. Farid,et al.  Biological electron transfer , 1995, Journal of bioenergetics and biomembranes.

[129]  P. Lindahl,et al.  Stoichiometric reductive titrations of Desulfovibrio gigas hydrogenase , 1995 .

[130]  E. Duin,et al.  Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum. , 1994, Biochemistry.

[131]  R. Thauer,et al.  Five new EPR signals assigned to nickel in methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum, strain Marburg , 1988 .

[132]  R. Cammack,et al.  ESR-detectable nickel and iron-sulphur centres in relation to the reversible activation of Desulfovibrio gigas hydrogenase , 1986 .

[133]  M. Teixeira,et al.  Unambiguous identification of the nickel EPR signal in 61Ni-enriched Desulfovibrio gigas hydrogenase. , 1982, Biochemical and biophysical research communications.

[134]  A. I. Krasna.  Hydrogenase: Properties and applications , 1979 .

[135]  M. Dupuis,et al.  Molecular dynamics study of the proposed proton transport pathways in [FeFe]-hydrogenase. , 2014, Biochimica et biophysica acta.

[136]  S. Shima,et al.  Preparation of [Fe]-hydrogenase from methanogenic archaea. , 2011, Methods in enzymology.

[137]  Daniel L DuBois,et al.  The roles of the first and second coordination spheres in the design of molecular catalysts for H2 production and oxidation. , 2009, Chemical Society reviews.

[138]  Erwin Reisner,et al.  Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology. , 2009, Chemical Society reviews.

[139]  A. L. Lacey,et al.  The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy , 2005, JBIC Journal of Biological Inorganic Chemistry.

[140]  E. Hatchikian,et al.  The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. I. Light sensitivity and magnetic hyperfine interactions as observed by electron paramagnetic resonance , 2005, JBIC Journal of Biological Inorganic Chemistry.

[141]  A. Volbeda,et al.  Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases , 2005, JBIC Journal of Biological Inorganic Chemistry.

[142]  S. Shima,et al.  UV-A/blue-light inactivation of the 'metal-free' hydrogenase (Hmd) from methanogenic archaea. , 2004, European journal of biochemistry.

[143]  W. Lubitz,et al.  An orientation-selected ENDOR and HYSCORE study of the Ni-C active state of Desulfovibrio vulgaris Miyazaki F hydrogenase , 2004, JBIC Journal of Biological Inorganic Chemistry.

[144]  M. Medina,et al.  Studies of light-induced nickel EPR signals in Desulfovibrio gigas hydrogenase , 1994 .