H Dobbek

Summary

Country: Germany

Publications

  1. pmc Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine
    H Dobbek
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 96:8884-9. 1999
  2. ncbi Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
    H Dobbek
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Science 293:1281-5. 2001
  3. pmc Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution
    Holger Dobbek
    Abteilung Strukturforschung, Max Planck Institut fur Biochemie, and Proteros Biostructures GmbH, D 82152 Martinsried, Germany Europe
    Proc Natl Acad Sci U S A 99:15971-6. 2002
  4. ncbi Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase
    Jae Hun Jeoung
    Laboratorium Proteinkristallographie and Forschungszentrum für Bio Makromoleküle, Universitat Bayreuth, D 95440 Bayreuth, Germany
    Science 318:1461-4. 2007
  5. pmc Assignment of individual metal redox states in a metalloprotein by crystallographic refinement at multiple X-ray wavelengths
    Oliver Einsle
    Institut fur Mikrobiologie und Genetik, Georg August Universitat Gottingen, 37077 Gottingen, Germany
    J Am Chem Soc 129:2210-1. 2007
  6. pmc Structural insights into methyltransfer reactions of a corrinoid iron-sulfur protein involved in acetyl-CoA synthesis
    Tatiana Svetlitchnaia
    Laboratorium Proteinkristallographie, Lehrstuhl fur Mikrobiologie, and Bayreuther Zentrum für Molekulare Biowissenschaften, Universitat Bayreuth, 95440 Bayreuth, Germany
    Proc Natl Acad Sci U S A 103:14331-6. 2006
  7. ncbi Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: physiological function, structure and mechanism of 8-hydroxycoumarin reduction
    Julia J Griese
    Laboratorium Proteinkristallographie, Universitat Bayreuth, Germany
    J Mol Biol 361:140-52. 2006
  8. ncbi Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans
    Marcus Resch
    Lehrstuhl fur Mikrobiologie, Bayreuther Zentrum für Molekulare Biowissenschaften, Universitat Bayreuth, 95440 Bayreuth, Germany
    J Biol Inorg Chem 10:518-28. 2005
  9. ncbi 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction
    Berta Maria Martins
    Laboratorium Proteinkristallographie, Universitat Bayreuth, Germany
    Structure 13:817-24. 2005
  10. pmc Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin
    Berta M Martins
    Max Planck Institut Biochemie, Strukturforschung, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 101:15645-9. 2004

Collaborators

  • B M Martins
  • Wolfgang Buckel
  • Oliver Einsle
  • DOUGLAS CHARLES REES
  • Jacques Meyer
  • A Messerschmidt
  • Jae Hun Jeoung
  • Ortwin Meyer
  • Vitali Svetlitchnyi
  • Insa Kather
  • Roman P Jakob
  • Gabriel Zoldak
  • Tatiana Svetlitchnaia
  • Julia J Griese
  • Marcus Resch
  • Robert Huber
  • Irena Bonin
  • Franz X Schmid
  • C Stefan Voertler
  • Nadine Wagener
  • Peter V Konarev
  • Erik Sedlak
  • Mathias Sprinzl
  • Lars Redecke
  • Diana A Pippig
  • Dmitri I Svergun
  • Stephan Schwarzinger
  • Bärbel Thiele
  • Vladimir Purvanov
  • Wolfram Meyer-Klaucke
  • Susanne Fetzner
  • Thomas Meins
  • Piero Römer

Detail Information

Publications17

  1. pmc Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine
    H Dobbek
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 96:8884-9. 1999
    ..A mechanism based on a structure with the bound suicide-substrate cyanide is suggested and displays the necessity of S-selanylcysteine for the catalyzed reaction...
  2. ncbi Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
    H Dobbek
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Science 293:1281-5. 2001
    ..The active-site clusters C and C' are novel, asymmetric [Ni-4Fe-5S] clusters. Their integral Ni ion, which is the likely site of CO oxidation, is coordinated by four sulfur ligands with square planar geometry...
  3. pmc Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution
    Holger Dobbek
    Abteilung Strukturforschung, Max Planck Institut fur Biochemie, and Proteros Biostructures GmbH, D 82152 Martinsried, Germany Europe
    Proc Natl Acad Sci U S A 99:15971-6. 2002
    ..The dinuclear [CuSMo(O)OH] cluster of CO dehydrogenase establishes a previously uncharacterized class of dinuclear molybdoenzymes containing the pterin cofactor...
  4. ncbi Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase
    Jae Hun Jeoung
    Laboratorium Proteinkristallographie and Forschungszentrum für Bio Makromoleküle, Universitat Bayreuth, D 95440 Bayreuth, Germany
    Science 318:1461-4. 2007
    ..It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidation and CO2 reduction at the Ni-Fe site of cluster C...
  5. pmc Assignment of individual metal redox states in a metalloprotein by crystallographic refinement at multiple X-ray wavelengths
    Oliver Einsle
    Institut fur Mikrobiologie und Genetik, Georg August Universitat Gottingen, 37077 Gottingen, Germany
    J Am Chem Soc 129:2210-1. 2007
  6. pmc Structural insights into methyltransfer reactions of a corrinoid iron-sulfur protein involved in acetyl-CoA synthesis
    Tatiana Svetlitchnaia
    Laboratorium Proteinkristallographie, Lehrstuhl fur Mikrobiologie, and Bayreuther Zentrum für Molekulare Biowissenschaften, Universitat Bayreuth, 95440 Bayreuth, Germany
    Proc Natl Acad Sci U S A 103:14331-6. 2006
    ..The conformation in the crystal structure shields the two open coordinations of cobalt and likely represents a resting state...
  7. ncbi Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: physiological function, structure and mechanism of 8-hydroxycoumarin reduction
    Julia J Griese
    Laboratorium Proteinkristallographie, Universitat Bayreuth, Germany
    J Mol Biol 361:140-52. 2006
    ..putida strains unable to degrade quinoline, it appears to have more than one physiological function and is an example of how enzymes with low substrate specificity can help to explain the variety of degradation pathways possible...
  8. ncbi Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans
    Marcus Resch
    Lehrstuhl fur Mikrobiologie, Bayreuther Zentrum für Molekulare Biowissenschaften, Universitat Bayreuth, 95440 Bayreuth, Germany
    J Biol Inorg Chem 10:518-28. 2005
    ..The other Mo-S group reacts with Cu(I), then Cu(2)S is released and an oxo group is introduced from water, yielding an inactive [MoO(3)] centre...
  9. ncbi 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction
    Berta Maria Martins
    Laboratorium Proteinkristallographie, Universitat Bayreuth, Germany
    Structure 13:817-24. 2005
    ..This creates an additional coordination site at the mononuclear Fe(II) ion and can open a pathway for dioxygen to bind in the substrate-containing active site...
  10. pmc Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin
    Berta M Martins
    Max Planck Institut Biochemie, Strukturforschung, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 101:15645-9. 2004
    ..Our results raise interesting questions regarding the mechanism of acyl-CoA dehydrogenases, which are involved in fatty acid oxidation, and address the divergent evolution of the ancestral common gene...
  11. ncbi Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase
    Irena Bonin
    Abteilung für Strukturforschung, Max Planck Institut fur Biochemie, 82152 Martinsried, Germany
    Structure 12:1425-35. 2004
    ..The active site protein variants QorE743V and QorE743D were analyzed to assess the catalytic role of E743...
  12. ncbi Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase
    Holger Dobbek
    Laboratorium für Proteinkristallographie, Universitat Bayreuth, Bayreuth, Germany
    J Am Chem Soc 126:5382-7. 2004
    ..These data suggest that the [Ni-4Fe-4S] cluster of CODHII(Ch) is an inactivated decomposition product originating from the [Ni-4Fe-5S] cluster...
  13. pmc A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans
    Vitali Svetlitchnyi
    Lehrstuhl fur Mikrobiologie, Universitat Bayreuth, D 95440 Bayreuth, Germany
    Proc Natl Acad Sci U S A 101:446-51. 2004
    ..2-A crystal structure of the dithionite-reduced monomer in an open conformation, and x-ray absorption spectroscopy...
  14. pmc Release factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies
    Gabriel Zoldak
    Department of Biochemistry, P J Safarik University Kosice, Slovakia
    Nucleic Acids Res 35:1343-53. 2007
    ..thermophilus and E. coli. Thermodynamic analyses and the X-ray scattering results for T. thermophilus RF2 in solution suggest that the compact conformation of RF2 resembles a physiological state in absence of the ribosome...
  15. ncbi HTHP: a novel class of hexameric, tyrosine-coordinated heme proteins
    Jae Hun Jeoung
    Laboratorium Proteinkristallographie, Universitat Bayreuth, Universitatsstrasse 30, 95447 Bayreuth, Germany
    J Mol Biol 368:1122-31. 2007
    ..We therefore propose that HTHP is the prototype of a new class of heme proteins...
  16. ncbi The molybdenum and tungsten cofactors: a crystallographic view
    Holger Dobbek
    Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Met Ions Biol Syst 39:227-63. 2002
  17. doi Increased folding stability of TEM-1 beta-lactamase by in vitro selection
    Insa Kather
    Laboratorium für Biochemie und Bayreuther, Zentrum für Molekulare Biowissenschaften, Universitat Bayreuth, 95440 Bayreuth, Germany
    J Mol Biol 383:238-51. 2008
    ..Such unfavorable van der Waals repulsions are not easily identified in crystal structures or by computational approaches, but they strongly reduce the conformational stability of a protein...