European Journal of Inorganic Chemistry

Cover image for Vol. 2011 Issue 7

Special Issue: Hydrogenases (Cluster Issue)

March 2011

Volume 2011, Issue 7

Pages 915–1171

Issue edited by: Marcetta Y. Darensbourg, Wolfgang Weigand

  1. Cover Picture

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
  2. Inside Cover

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
    1. Cyanide and Carbon Monoxide Ligand Formation in Hydrogenase Biosynthesis

      Kevin D. Swanson, Benjamin R. Duffus, Trevor E. Beard, John W. Peters and Joan B. Broderick

      Article first published online: 23 FEB 2011 | DOI: 10.1002/ejic.201190020

  3. Editorials

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
    1. Hydrogenases (Eur. J. Inorg. Chem. 7/2011) (pages 917–918)

      Marcetta Y. Darensbourg and Wolfgang Weigand

      Article first published online: 21 FEB 2011 | DOI: 10.1002/ejic.201190017

  4. Essay

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
    1. The Global Hydrogen Cycle

      Hydrogenases and the Global H2 Cycle (pages 919–921)

      Rudolf Kurt Thauer

      Article first published online: 10 FEB 2011 | DOI: 10.1002/ejic.201001255

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      The collection of contributions in this cluster issue on hydrogenases deals with the mechanism, biosynthesis, evolution, and application of hydrogenases. This essay introduces the reader to the global hydrogen cycle and the types of hydrogenases that are used for proton reduction and dihydrogen oxidation.

  5. Graphical Abstract

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
  6. News

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
  7. Microreviews

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
    1. H-Cluster Biosynthesis

      Cyanide and Carbon Monoxide Ligand Formation in Hydrogenase Biosynthesis (pages 935–947)

      Kevin D. Swanson, Benjamin R. Duffus, Trevor E. Beard, John W. Peters and Joan B. Broderick

      Article first published online: 20 JAN 2011 | DOI: 10.1002/ejic.201001056

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      Hydrogenase active site (H-cluster) ligands are synthesized by maturation enzymes to generate an active enzyme capable of catalyzing the formation or oxidation of hydrogen. This review discusses the differenthydrogenase maturation systems, and it also describes cyanide and carbon monoxide biosynthetic systems. Particular focus is given to [FeFe]-hydrogenase H-cluster biosynthesis.

    2. Biohydrogen Production

      You have full text access to this OnlineOpen article
      Nickel–Iron–Selenium Hydrogenases – An Overview (pages 948–962)

      Carla S. A. Baltazar, Marta C. Marques, Cláudio M. Soares, Antonio M. DeLacey, Inês A. C. Pereira and Pedro M. Matias

      Article first published online: 10 JAN 2011 | DOI: 10.1002/ejic.201001127

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      Herein we review the distribution, biochemical, catalytic, spectroscopic and structural properties of known [NiFeSe] hydrogenases of the Hys, Vhu and Fru classes and report on active-site models for the Vhu and Fru enzymes, for which there is no structural information. Hys hydrogenases are attractive catalysts for technological applications such as biohydrogen production.

    3. Hydrogen Activation

      Structure and Function of [Fe]-Hydrogenase and its Iron–Guanylylpyridinol (FeGP) Cofactor (pages 963–972)

      Seigo Shima and Ulrich Ermler

      Article first published online: 17 DEC 2010 | DOI: 10.1002/ejic.201000955

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      [Fe]-hydrogenase catalyzes the reversible reduction of methenyltetrahydromethanopterin with H2. This third type of hydrogenase contains a unique iron–guanylylpyridinol (FeGP) cofactor. In the closed model of the enzyme, the iron ligation site trans to the acyl carbon atom is next to the C14a carbon atom and is therefore considered to be the H2 binding site.

    4. Models for the [NiFe] Hydrogenase

      Thiolate-Bridged Iron–Nickel Models for the Active Site of [NiFe] Hydrogenase (pages 973–985)

      Yasuhiro Ohki and Kazuyuki Tatsumi

      Article first published online: 30 DEC 2010 | DOI: 10.1002/ejic.201001087

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      [NiFe] hydrogenase is the most common type among the currently known hydrogenases, and its active site consists of an “organometallic” Fe–Ni complex supported by cysteinyl thiolate ligands. This review presents an overview of the synthesis, properties, and reactions of thiolate-bridged iron–nickel complexes that model the active site of [NiFe] hydrogenase.

    5. [FeFe] Hydrogenases

      Diiron Dichalcogenolato (Se and Te) Complexes: Models for the Active Site of [FeFe] Hydrogenase (pages 986–993)

      Mohammad K. Harb, Ulf-Peter Apfel, Takahiro Sakamoto, Mohammad El-khateeb and Wolfgang Weigand

      Article first published online: 31 JAN 2011 | DOI: 10.1002/ejic.201001112

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      [FeFe] hydrogenase models containing different chalcogens such as S, Se, or Te are reviewed and compared with diiron dithiolato compound analogues for their ability to catalyze the formation of H2 from weak acids.

    6. Sulfoxygenation

      Sulfoxygenation of Active Site Models of [NiFe] and [FeFe] Hydrogenases – A Commentary on Possible Chemical Models of Hydrogenase Enzyme Oxygen Sensitivity (pages 994–1004)

      Marcetta Y. Darensbourg and Wolfgang Weigand

      Article first published online: 3 FEB 2011 | DOI: 10.1002/ejic.201001148

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      An overview of the oxygen sensitivity of [NiFe] and [FeFe] hydrogenase and studies of oxygen reactivity with synthetic analogues of the enzyme active site are presented. Discrete S-oxygenate complexes that maintain the Ni-S or Fe-S connectivity could signify reversible oxygen damage, and a protective, “antioxidant” role of the sulfur atoms in the active sites.

    7. Hydrogen Production

      Solar Hydrogen Evolution with Hydrogenases: From Natural to Hybrid Systems (pages 1005–1016)

      Erwin Reisner

      Article first published online: 3 DEC 2010 | DOI: 10.1002/ejic.201000986

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      Hydrogenases are enzymes that catalyze the reversible production of H2 from aqueous protons at an iron or nickel/iron active site. The utilization of these enzymes invivo and by man-made hybrid systems for photochemical hydrogen production is reviewed.

    8. Molecular Electrocatalysts

      Molecular Electrocatalysts for the Oxidation of Hydrogen and the Production of Hydrogen – The Role of Pendant Amines as Proton Relays (pages 1017–1027)

      Daniel L. DuBois and R. Morris Bullock

      Article first published online: 4 JAN 2011 | DOI: 10.1002/ejic.201001081

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      Pendant amines function as proton relays in molecular electrocatalysts, facilitating transfer of protons to and from the metal. A series of NiII complexes with diphosphanes bearing pendant amines are catalysts for oxidation of H2, and a related series of NiII and CoII complexes catalyze the production of H2 by reduction of protons.

  8. Short Communications

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
    1. Azadithiolate Complexes

      A New Route to Azadithiolato Complexes (pages 1029–1032)

      Raja Angamuthu, Maria E. Carroll, Maya Ramesh and Thomas B. Rauchfuss

      Article first published online: 14 JAN 2011 | DOI: 10.1002/ejic.201001208

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      Azadithiolate (S–CH2–NH–CH2–S) is one of the unusual cofactors of the [FeFe]-hydrogenase enzyme. Reaction of [(MeC5H4)2Ti(SH)2] with cyclic imines with the formula (CH2NR)3 gives 2-aza-1,3-dithiolato chelate complexes [(MeC5H4)2Ti{(SCH2)2NR}]. These compounds demonstrate that azadithiolate ligands can exist on mononuclear metal centers.

    2. [FeFe]-Hydrogenase

      [FeFe]-Hydrogenase Models: Unexpected Variation in Protonation Rate between Dithiolate Bridge Analogues (pages 1033–1037)

      Aušra Jablonskytė, Joseph A. Wright and Christopher J. Pickett

      Article first published online: 15 NOV 2010 | DOI: 10.1002/ejic.201001072

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      The identity of the central atom in the dithiolate bridge of the [FeFe]-hydrogenase {2Fe2S} subsite is a key question in the activity of the enzyme. Protonation kinetics studies on the simple model Fe2(μ-odt)(CO)4(PMe3)2 (odt = 2-oxapropane-1,3-dithiolate) show that the identiy of this atom has significant implications for the rate of protonation in model complexes.

    3. Bioinspired Organometallic Molecules

      Diiron Complexes with a [2Fe3S] Core Related to the Active Site of [FeFe]H2ases (pages 1038–1042)

      Kévin Charreteur, Jean-François Capon, Frédéric Gloaguen, François Y. Pétillon, Philippe Schollhammer and Jean Talarmin

      Article first published online: 19 OCT 2010 | DOI: 10.1002/ejic.201000984

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      Molecules in which a [2Fe3S] core is combined with six-membered heterocyclic sulfur ligands with well positioned heteroatoms, such as 1,4-dithiane (C4H8S2) and 1,4-thioxane (C4H8OS) and an unexpected [4Fe8S] cluster have been elaborated.

  9. Full Papers

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Editorials
    5. Essay
    6. Graphical Abstract
    7. News
    8. Microreviews
    9. Short Communications
    10. Full Papers
    1. Calculations on Hydrogenases

      Magnetic Properties of [FeFe]-Hydrogenases: A Theoretical Investigation Based on Extended QM and QM/MM Models of the H-Cluster and Its Surroundings (pages 1043–1049)

      Claudio Greco, Alexey Silakov, Maurizio Bruschi, Ulf Ryde, Luca De Gioia and Wolfgang Lubitz

      Article first published online: 20 JAN 2011 | DOI: 10.1002/ejic.201001058

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      Magnetic properties of [FeFe]-hydrogenases are computed, based on purely QM and on QM/MM enzyme models. Calculated g values are highly dependent on the broken-symmetry coupling scheme and on the level of theory used; theoretical hyperfine couplings are more stable, and indicate the presence of an exogenous ligand like a water molecule in the partially oxidized active site.

    2. Enzyme Models

      Artificial [FeFe]-Hydrogenase: On Resin Modification of an Amino Acid to Anchor a Hexacarbonyldiiron Cluster in a Peptide Framework (pages 1050–1055)

      Souvik Roy, Sandip Shinde, G. Alexander Hamilton, Hilairy E. Hartnett and Anne K. Jones

      Article first published online: 17 NOV 2010 | DOI: 10.1002/ejic.201000979

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      A general method for modification of a primary amine in peptides to create a dithiol anchor for metalloclusters is presented. The dithiol side chain is then used to construct a peptide-ligated [FeFe]-hydrogenase model.

    3. Photodissociation in Fe Hydrogenases

      Unraveling the Electronic Properties of the Photoinduced States of the H-Cluster in the [FeFe] Hydrogenase from D. desulfuricans (pages 1056–1066)

      Alexey Silakov, Edward J. Reijerse and Wolfgang Lubitz

      Article first published online: 12 JAN 2011 | DOI: 10.1002/ejic.201001080

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      Photodissociation of the CO ligands of the active site of the [FeFe] hydrogenase from D. desulfuricans was studied by advanced pulse EPR methods. Two light-induced states were found. One of them is characterized by removal of the external CO ligands, while another by removal of the bridging CO ligand. The electronic structure of the latter was found to be different from the other EPR active states.

    4. [NiFe] Hydrogenase

      The Hydrogenase Subcomplex of the NAD+-Reducing [NiFe] Hydrogenase from Ralstonia eutropha – Insights into Catalysis and Redox Interconversions (pages 1067–1079)

      Lars Lauterbach, Juan Liu, Marius Horch, Phillip Hummel, Alexander Schwarze, Michael Haumann, Kylie A. Vincent, Oliver Lenz and Ingo Zebger

      Article first published online: 2 FEB 2011 | DOI: 10.1002/ejic.201001053

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      The engineered subcomplex, HoxHY, of the NAD+-reducing soluble hydrogenase from Ralstonia eutropha is catalytically active for H+ reduction and H2 oxidation. Spectroscopic analyses revealed one FeS cluster, a [NiFe] active site with standard ligation, and substoichiometric amounts of FMN. Redox dependent transitions between active and inactive states were examined by IR and electrochemistry.

    5. [FeFe]-Hydrogenase Model

      Density Functional Calculations on Protonation of the [FeFe]-Hydrogenase Model Complex Fe2(μ-pdt)(CO)4(PMe3)2 and Subsequent Isomerization Pathways (pages 1080–1093)

      Caiping Liu, Jamie N. T. Peck, Joseph A. Wright, Christopher J. Pickett and Michael B. Hall

      Article first published online: 26 JAN 2011 | DOI: 10.1002/ejic.201001085

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      The initial protonation of a diiron model complex occurs terminally at one Fe on the basal/basal isomer 1D rather than the apical/basal isomer 1A. Then, rearrangement occurs to the bridging species 2A, which then rearranges more slowly through two competing paths to the most stable isomer, 2D.

    6. Hydrogenase Models

      Cp*-Ruthenium–Nickel-Based H2-Evolving Electrocatalysts as Bio-inspired Models of NiFe Hydrogenases (pages 1094–1099)

      Sigolène Canaguier, Marc Fontecave and Vincent Artero

      Article first published online: 14 DEC 2010 | DOI: 10.1002/ejic.201000944

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      The introduction of a pentamethylcyclopentadienyl (Cp*) ligand into the coordination sphere of Ru has led to the preparation of a new series of active and robust Ni–Ru catalysts for the evolution of H2 as mimics of the active site of NiFe hydrogenases.

    7. Synthesis of [3Fe2S] from [2Fe2S]

      Synthesis of a [3Fe2S] Cluster with Low Redox Potential from [2Fe2S] Hydrogenase Models: Electrochemical and Photochemical Generation of Hydrogen (pages 1100–1105)

      Weiming Gao, Junliang Sun, Mingrun Li, Torbjörn Åkermark, Kristina Romare, Licheng Sun and Björn Åkermark

      Article first published online: 5 JAN 2011 | DOI: 10.1002/ejic.201000872

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      An unexpected and efficient transformation of the [2Fe2S] complexes 1a and 1b into complex [3Fe2S(dppv)2] (2) [dppv = bis(cis-Ph2PCH=CHPPh2)] is described. Under acidic conditions, cyclic voltammetry experiments showed electrochemical activity for hydride 3, formed by protonation of complex 2, at –1 V vs. Fc/Fc+ and catalysis of hydrogen evolution at –1.23 V vs. Fc/Fc+.

    8. Bioinorganic Iron Carbonyls

      Comparing the Reactivity of Benzenedithiolate- versus Alkyldithiolate-Bridged Fe2(CO)6 Complexes with Competing Ligands (pages 1106–1111)

      Daniel Streich, Michael Karnahl, Yeni Astuti, Clyde W. Cady, Leif Hammarström, Reiner Lomoth and Sascha Ott

      Article first published online: 26 JAN 2011 | DOI: 10.1002/ejic.201001152

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      Exposure of [(μ-bdt)Fe2(CO)6], (bdt)1, to secondary amines or dmf results in major structural changes of the complex and formation of a magnetically uncoupled FeI species that carries the bdt and CO ligands. This reactivity contrasts that of [(μ-edt)Fe2(CO)6], (edt)1, and [(μ-pdt)Fe2(CO)6], (pdt)1, which are unreactive under identicalconditions (bdt, edt, pdt = benzene-, ethyl-, propyldithiolate, respectively).

    9. Mimics of [FeFe]-Hydrogenases

      Diiron Complexes with Pendant Phenol Group(s) as Mimics of the Diiron Subunit of [FeFe]-Hydrogenase: Synthesis, Characterisation, and Electrochemical Investigation (pages 1112–1120)

      Ying Tang, Zhenhong Wei, Wei Zhong and Xiaoming Liu

      Article first published online: 11 JAN 2011 | DOI: 10.1002/ejic.201001092

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      The bridging linkages of the diiron model complexes govern directly their electrochemistry and electrocatalytic reduction ofprotons, as the linkages determine thenature of the coupled chemical reaction in the ECE processes.

    10. [FeFe]-Hydrogenase

      Further Characterization of the [FeFe]-Hydrogenase Maturase HydG (pages 1121–1127)

      Cécile Tron, Mickaël V. Cherrier, Patricia Amara, Lydie Martin, Francois Fauth, Edmundo Fraga, Mélanie Correard, Marc Fontecave, Yvain Nicolet and Juan C. Fontecilla-Camps

      Article first published online: 2 FEB 2011 | DOI: 10.1002/ejic.201001101

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      We have explored the CO/CN synthesis catalyzed by [FeFe]-hydrogenase maturase HydG with site-directed mutants, and have performed functional studies, SAXS spectroscopy and homology modeling. We conclude that whereas CN is made in the active site-containing TIM-barrel domain, the CO precursor follows an internal path from this site to a catalytic [4Fe-4S] cluster in the tightly bound C-terminal domain.

    11. Electrocatalytic Proton Reduction

      XAFS and DFT Characterisation of Protonated Reduced Fe Hydrogenase Analogues and Their Implications for Electrocatalytic Proton Reduction (pages 1128–1137)

      Mun Hon Cheah and Stephen P. Best

      Article first published online: 2 FEB 2011 | DOI: 10.1002/ejic.201001099

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      The two reaction paths for dihydrogen elimination from two-electron-reduced, protonated diiron compounds related to the hydrogenase H-cluster available from DFT calculations are considered in terms of a range of spectroscopic, electrochemical, DFT and XAFS studies of [FeH(CO)3](μ-PPh3)2. Limitations are evident for the transition states associated with both of the calculated reaction paths.

    12. Specific Immobilization of Proteins

      Tailor-Made Modification of a Gold Surface for the Chemical Binding of a High-Activity [FeFe] Hydrogenase (pages 1138–1146)

      Henning Krassen, Sven T. Stripp, Nadine Böhm, Albrecht Berkessel, Thomas Happe, Kenichi Ataka and Joachim Heberle

      Article first published online: 2 FEB 2011 | DOI: 10.1002/ejic.201001190

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      We demonstrated the specific binding of a [FeFe] hydrogenase to a modified gold surface by IR spectroscopy. A novel linker thiol, 1-(10-mercaptodecyl)-1′-benzyl-4,4′-bipyridinium dibromide (MBBP), was synthesized and characterized. The hydrogenase layer releases H2 at –450 mV vs. NHE, which was probed by electrochemistry and gas chromatography. Protein binding and electron transfer are discussed.

    13. Protonation of Hydrogenases

      Favorable Protonation of the (μ-edt)[Fe2(PMe3)4(CO)2(H-terminal)]+ Hydrogenase Model Complex Over Its Bridging μ-H Counterpart: A Spectroscopic and DFT Study (pages 1147–1154)

      Mary Grace I. Galinato, C. Matthew Whaley, Dean Roberts, Peng Wang and Nicolai Lehnert

      Article first published online: 20 JAN 2011 | DOI: 10.1002/ejic.201001037

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      A theoretical and spectroscopic study of the preferential protonation of the catalytically active terminal hydride (H-term) isomer of the hydrogenase model complex (μ-edt)[Fe2(PMe3)4(CO)2(H)]+ is presented. Relative to the bridging hydride isomer, H-term has a lower activation energy barrier for protonation, due to a key MO that shows a relatively strong hydride (1s) contribution.

    14. [FeFe] Hydrogenases

      Influence of a Redox-Active Phosphane Ligand on the Oxidations of a Diiron Core Related to the Active Site of Fe-Only Hydrogenase (pages 1155–1162)

      Yu-Chiao Liu, Chia-Hsin Lee, Gene-Hsiang Lee and Ming-Hsi Chiang

      Article first published online: 24 JAN 2011 | DOI: 10.1002/ejic.201000972

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      Ligation of mppf to the {Fe2S2} unitalters the oxidation levels of the Fe2 coreand improves stability of the oxidizedspecies.

    15. Oxygen-Sensitivity of Hydrogenases

      Oxygen Coordination to the Active Site of Hmd in Relation to [FeFe] Hydrogenase (pages 1163–1171)

      Martin T. Stiebritz, Arndt R. Finkelmann and Markus Reiher

      Article first published online: 4 FEB 2011 | DOI: 10.1002/ejic.201001161

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      A DFT study of energy differences in oxygen coordination at the active sites of [FeFe] and monoiron (Hmd) hydrogenase reveals that first shell ligands determine O2 coordination to the Hmd active site. Changing the first ligand shell but keeping the ligand sphere the same causes the oxygen coordination to become endo- or exothermic, which explains the difference in oxygen sensitivity of Hmd and [FeFe] hydrogenases.

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