Reiner Hedderich

Summary

Affiliation: Philipps University
Country: Germany

Publications

  1. ncbi request reprint Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction
    Evert C Duin
    Max Planck Institut für Terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps Universitat, Karl von Frisch Strasse, D 35043, Marburg, Germany
    FEBS Lett 512:263-8. 2002
  2. ncbi request reprint Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I
    Reiner Hedderich
    Max Planck Institut fur terrestrische Mikrobiologie, Karl von Frisch Strasse, D 35043 Marburg, Germany
    J Bioenerg Biomembr 36:65-75. 2004
  3. pmc A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from Methanothermobacter marburgensis
    Nils Hamann
    Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Strasse, D 35043 Marburg, Germany
    Biochemistry 46:12875-85. 2007
  4. ncbi request reprint Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
    Reiner Hedderich
    Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Strasse, D 35043 Marburg, Germany
    Biol Chem 386:961-70. 2005
  5. ncbi request reprint Energy-converting [NiFe] hydrogenases: more than just H2 activation
    Reiner Hedderich
    Max Planck Institut fur terrestrische Mikrobiologie, Marburg, Germany
    J Mol Microbiol Biotechnol 10:92-104. 2005
  6. ncbi request reprint F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification
    Henning Seedorf
    Max Planck Institut für terrestrische Mikrobiologie und Laboratorium für Mikrobiologie des Fachbereichs Biologie, Philipps Universitat, Karl von Frisch Strasse, 35043 Marburg, Germany
    Arch Microbiol 182:126-37. 2004
  7. ncbi request reprint Two distinct heterodisulfide reductase-like enzymes in the sulfate-reducing archaeon Archaeoglobus profundus
    Gerd J Mander
    Max Planck Institut for Terrestrial Microbiology, Marburg, Germany
    Eur J Biochem 271:1106-16. 2004
  8. ncbi request reprint Assignment of the [4Fe-4S] clusters of Ech hydrogenase from Methanosarcina barkeri to individual subunits via the characterization of site-directed mutants
    Lucia Forzi
    Max Planck Institute for Terrestrial Microbiology, Marburg, Germany
    FEBS J 272:4741-53. 2005
  9. pmc The CCG-domain-containing subunit SdhE of succinate:quinone oxidoreductase from Sulfolobus solfataricus P2 binds a [4Fe-4S] cluster
    Nils Hamann
    Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Strasse, 35043, Marburg, Germany
    J Biol Inorg Chem 14:457-70. 2009
  10. doi request reprint Methanogenic archaea: ecologically relevant differences in energy conservation
    Rudolf K Thauer
    Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Strasse, D 35043 Marburg, Germany
    Nat Rev Microbiol 6:579-91. 2008

Collaborators

Detail Information

Publications29

  1. ncbi request reprint Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction
    Evert C Duin
    Max Planck Institut für Terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps Universitat, Karl von Frisch Strasse, D 35043, Marburg, Germany
    FEBS Lett 512:263-8. 2002
    ..The catalytic mechanism of HDR is discussed in light of the crystallographic and spectroscopic studies of the related chloroplast ferredoxin:thioredoxin reductase class of disulfide reductases...
  2. ncbi request reprint Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I
    Reiner Hedderich
    Max Planck Institut fur terrestrische Mikrobiologie, Karl von Frisch Strasse, D 35043 Marburg, Germany
    J Bioenerg Biomembr 36:65-75. 2004
    ..As complex I these hydrogenases function as ion pumps and have therefore been designated as energy-converting [NiFe] hydrogenases...
  3. pmc A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from Methanothermobacter marburgensis
    Nils Hamann
    Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Strasse, D 35043 Marburg, Germany
    Biochemistry 46:12875-85. 2007
    ..In addition, Zn K-edge X-ray absorption spectroscopy identified an isolated Zn site with an S3(O/N)1 geometry in HdrB and the HDR holoenzyme. The N-terminal CCG domain is suggested to provide ligands to the Zn site...
  4. ncbi request reprint Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
    Reiner Hedderich
    Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Strasse, D 35043 Marburg, Germany
    Biol Chem 386:961-70. 2005
    ..The formal thiyl radical generated by the initial one-electron reduction of the disulfide is stabilized via reduction and coordination of the resultant thiol to the [4Fe-4S] cluster...
  5. ncbi request reprint Energy-converting [NiFe] hydrogenases: more than just H2 activation
    Reiner Hedderich
    Max Planck Institut fur terrestrische Mikrobiologie, Marburg, Germany
    J Mol Microbiol Biotechnol 10:92-104. 2005
    ..These hydrogenases have therefore been designated as energy-converting [NiFe] hydrogenases...
  6. ncbi request reprint F420H2 oxidase (FprA) from Methanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification
    Henning Seedorf
    Max Planck Institut für terrestrische Mikrobiologie und Laboratorium für Mikrobiologie des Fachbereichs Biologie, Philipps Universitat, Karl von Frisch Strasse, 35043 Marburg, Germany
    Arch Microbiol 182:126-37. 2004
    ..The presence of F(420)H(2) oxidase in methanogenic archaea may explain why some methanogens, e.g., the Methanobrevibacter species in the termite hindgut, cannot only tolerate but thrive under microoxic conditions...
  7. ncbi request reprint Two distinct heterodisulfide reductase-like enzymes in the sulfate-reducing archaeon Archaeoglobus profundus
    Gerd J Mander
    Max Planck Institut for Terrestrial Microbiology, Marburg, Germany
    Eur J Biochem 271:1106-16. 2004
    ..The oxidized enzyme exhibited an unusual EPR spectrum with gxyz = 2.014, 1.939 and 1.895 similar to that observed for oxidized Hme and Hdr. Upon reduction with H2 this signal was no longer detectable...
  8. ncbi request reprint Assignment of the [4Fe-4S] clusters of Ech hydrogenase from Methanosarcina barkeri to individual subunits via the characterization of site-directed mutants
    Lucia Forzi
    Max Planck Institute for Terrestrial Microbiology, Marburg, Germany
    FEBS J 272:4741-53. 2005
    ..The pH-dependence of these two [4Fe-4S] clusters suggests that they simultaneously mediate electron and proton transfer and thus could be an essential part of the proton-translocating machinery...
  9. pmc The CCG-domain-containing subunit SdhE of succinate:quinone oxidoreductase from Sulfolobus solfataricus P2 binds a [4Fe-4S] cluster
    Nils Hamann
    Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Strasse, 35043, Marburg, Germany
    J Biol Inorg Chem 14:457-70. 2009
    ..Since cysteine residues in SdhE are restricted to the two CCG domains, we conclude that these domains provide the ligands to both the iron-sulfur cluster and the zinc site...
  10. doi request reprint Methanogenic archaea: ecologically relevant differences in energy conservation
    Rudolf K Thauer
    Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Strasse, D 35043 Marburg, Germany
    Nat Rev Microbiol 6:579-91. 2008
    ....
  11. ncbi request reprint A multisubunit membrane-bound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis
    Basem Soboh
    Max Planck Institut fur terrestrische Mikrobiologie, Karl von Frisch Strasse, D 35043 Marburg, Germany
    Microbiology 150:2451-63. 2004
    ..These results indicate a regulation in response to the p(H(2))...
  12. ncbi request reprint CO2 reduction to the level of formylmethanofuran in Methanosarcina barkeri is non-energy driven when CO is the electron donor
    Alexander Stojanowic
    Max Planck Institut fur terrestrische Mikrobiologie, Karl von Frisch Strasse, D 35043 Marburg, Germany
    FEMS Microbiol Lett 235:163-7. 2004
    ....
  13. ncbi request reprint The membrane-bound [NiFe]-hydrogenase (Ech) from Methanosarcina barkeri: unusual properties of the iron-sulphur clusters
    Sergei Kurkin
    Swammerdam Institute for Life Sciences, Biochemistry, University of Amsterdam, the Netherlands Max Planck Institut für Terrestrische Mikrobiologie, Marburg, Germany
    Eur J Biochem 269:6101-11. 2002
    ..The possible relevance of these properties for the function of this proton-pumping [NiFe]-hydrogenase is discussed...
  14. doi request reprint Profiling the outer membrane proteome during growth and development of the social bacterium Myxococcus xanthus by selective biotinylation and analyses of outer membrane vesicles
    Jörg Kahnt
    Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Str, Marburg, Germany
    J Proteome Res 9:5197-208. 2010
    ..The luminal load of OMV was enriched for proteins with hydrolytic functions. Our data suggest that OMV have functions in predation and possibly in transfer of intercellular signaling molecules between cells...
  15. ncbi request reprint Purification and catalytic properties of a CO-oxidizing:H2-evolving enzyme complex from Carboxydothermus hydrogenoformans
    Basem Soboh
    Max Planck Institut fur terrestrische Mikrobiologie, Karl von Frisch Strasse, Marburg, Germany
    Eur J Biochem 269:5712-21. 2002
    ..The exergonic redox reaction catalyzed by the enzyme complex in vivo has to be coupled to energy conservation, most likely via the generation of a proton motive force...
  16. ncbi request reprint Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [33S]coenzyme M-treated enzyme
    Evert C Duin
    Max Planck Institut fur terrestrische Mikrobiologie, Karl von Frisch Strasse, D 35043 Marburg, Germany
    FEBS Lett 538:81-4. 2003
    ..The results provide compelling evidence for a direct binding of CoM-SH to the [4Fe-4S] cluster in the active site of the enzyme...
  17. pmc Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    Jörn Meuer
    Max Planck Institut fur terrestrische Mikrobiologie, 35043 Marburg, Germany
    Proc Natl Acad Sci U S A 99:5632-7. 2002
    ..Thus, in vivo genetic analysis has led to the identification of the electron donor of this key initial step of methanogenesis...
  18. ncbi request reprint Physiological role of the F420-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis
    Alexander Stojanowic
    Max Planck Institut fur terrestrische Mikrobiologie, Karl von Frisch Strasse, 35043, Marburg, Germany
    Arch Microbiol 180:194-203. 2003
    ....
  19. ncbi request reprint X-ray structure of the gamma-subunit of a dissimilatory sulfite reductase: fixed and flexible C-terminal arms
    Gerd J Mander
    Max Planck Institut fur terrestrische Mikrobiologie, Karl von Frisch Str, D 35043 Marburg, Germany
    FEBS Lett 579:4600-4. 2005
    ..aerophilum DsrC. The functional relevance of both conformations and of a potentially redox-active disulfide bond between the strictly invariant Cys103 and Cys114 are discussed...
  20. ncbi request reprint Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea
    Gerd J Mander
    Max Planck Institut fur terrestrische Mikrobiologie, Marburg, Germany
    Eur J Biochem 269:1895-904. 2002
    ..Hence, Hdr and the A. fulgidus enzyme not only share sequence similarity, but may also have a similar active site and a similar catalytic function...
  21. pmc Bioinformatics and experimental analysis of proteins of two-component systems in Myxococcus xanthus
    Xingqi Shi
    Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Karl von Frisch Str, 35043 Marburg, Germany
    J Bacteriol 190:613-24. 2008
    ....
  22. ncbi request reprint Sodium ion pumps and hydrogen production in glutamate fermenting anaerobic bacteria
    Clara D Boiangiu
    Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps Universitat, Marburg, Germany
    J Mol Microbiol Biotechnol 10:105-19. 2005
    ..The reduced ferredoxin is required for hydrogen production and the activation of radical enzymes. Further examples show that reduced ferredoxin is an agent, whose reducing energy is about 1 ATP 'richer' than that of NADH...
  23. pmc The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis
    Wolfgang F Fricke
    Göttingen Genomics Laboratory, Institute of Microbiology and Genetics, Georg August University, Grisebachstr 8, D 37077 Gottingen, Germany
    J Bacteriol 188:642-58. 2006
    ....
  24. ncbi request reprint Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase
    Jacob E Shokes
    Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602 2556, USA
    FEBS Lett 579:1741-4. 2005
    ..Se K edge extended X-ray absorption fine structure confirms a direct interaction of the Se in CoM-SeH-treated HDR with an Fe atom of the Fe-S cluster at an Fe-Se distance of 2.4A...
  25. ncbi request reprint LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis
    Boran Altincicek
    Jomaa Pharmaka GmbH, Frankfurter Strasse 50, 35392, Giessen, Germany
    FEBS Lett 532:437-40. 2002
    ..The maximal specific activity of 6.6+/-0.3 micromol x min(-1) x mg(-1) protein was determined at pH 7.5 and 60 degrees C. The k(cat) value of the LytB protein was 3.7+/-0.2 s(-1) and the K(m) value for HMBPP was 590+/-60 microM...
  26. pmc The genome of M. acetivorans reveals extensive metabolic and physiological diversity
    James E Galagan
    Whitehead Institute Center for Genome Research, Cambridge, Massachusetts 02141, USA
    Genome Res 12:532-42. 2002
    ..acetivorans a powerful model organism for the study of archaeal biology. [Sequence, data, annotations and analyses are available at http://www-genome.wi.mit.edu/.]..
  27. ncbi request reprint (57)Fe ENDOR spectroscopy on the iron-sulfur cluster involved in substrate reduction of heterodisulfide reductase
    Marina Bennati
    Institute of Physical and Theoretical Chemistry and Center for Biomolecular Magnetic Resonance, J W Goethe University of Frankfurt, D 60439 Frankfurt, Germany
    J Am Chem Soc 126:8378-9. 2004
    ..We find direct evidence for a [4Fe-4S]3+ cluster, and we determine the sign of the 57Fe hyperfine couplings. The 57Fe isotropic hfc values suggest a complex interaction between the cluster and the CoM-SH substrate...
  28. ncbi request reprint Determination of a novel structure by a combination of long-wavelength sulfur phasing and radiation-damage-induced phasing
    Manfred S Weiss
    EMBL Hamburg Outstation, c o DESY, Notkestrasse 85, D 22603 Hamburg, Germany
    Acta Crystallogr D Biol Crystallogr 60:686-95. 2004
    ..A computational correction for the radiation damage was found to significantly improve the success rate in determining the heavy-atom substructure and to improve phasing and refinement statistics...
  29. ncbi request reprint Functional characterization of GcpE, an essential enzyme of the non-mevalonate pathway of isoprenoid biosynthesis
    Ann Kristin Kollas
    Biochemisches Institut, Justus Liebig Universitat Giessen, Friedrichstrasse 24, 35392, Giessen, Germany
    FEBS Lett 532:432-6. 2002
    ..The maximal specific activity was 0.6 micromol x min(-1) x mg(-1) at pH 7.5 and 55 degrees C. The kcat value was 0.4 s(-1) and the K(m) value for HMBPP 0.42 mM...