Crossref journal-article
American Society for Microbiology
Journal of Bacteriology (235)
Abstract

ABSTRACT Two monofunctional NiFeS carbon monoxide (CO) dehydrogenases, designated CODH I and CODH II, were purified to homogeneity from the anaerobic CO-utilizing eubacterium Carboxydothermus hydrogenoformans . Both enzymes differ in their subunit molecular masses, N-terminal sequences, peptide maps, and immunological reactivities. Immunogold labeling of ultrathin sections revealed both CODHs in association with the inner aspect of the cytoplasmic membrane. Both enzymes catalyze the reaction CO + H 2 O → CO 2 + 2 e − + 2 H + . Oxidized viologen dyes are effective electron acceptors. The specific enzyme activities were 15,756 (CODH I) and 13,828 (CODH II) μmol of CO oxidized min −1 mg −1 of protein (methyl viologen, pH 8.0, 70°C). The two enzymes oxidize CO very efficiently, as indicated by k cat /K m values at 70°C of 1.3 · 10 9 M −1 CO s −1 (CODH I) and 1.7 · 10 9 M −1 CO s −1 (CODH II). The apparent K m values at pH 8.0 and 70°C are 30 and 18 μM CO for CODH I and CODH II, respectively. Acetyl coenzyme A synthase activity is not associated with the enzymes. CODH I (125 kDa, 62.5-kDa subunit) and CODH II (129 kDa, 64.5-kDa subunit) are homodimers containing 1.3 to 1.4 and 1.7 atoms of Ni, 20 to 22 and 20 to 24 atoms of Fe, and 22 and 19 atoms of acid-labile sulfur, respectively. Electron paramagnetic resonance (EPR) spectroscopy revealed signals indicative of [4Fe-4S] clusters. Ni was EPR silent under any conditions tested. It is proposed that CODH I is involved in energy generation and that CODH II serves in anabolic functions.

Bibliography

Svetlitchnyi, V., Peschel, C., Acker, G., & Meyer, O. (2001). Two Membrane-Associated NiFeS-Carbon Monoxide Dehydrogenases from the Anaerobic Carbon-Monoxide-Utilizing Eubacterium Carboxydothermus hydrogenoformans. Journal of Bacteriology, 183(17), 5134–5144.

Authors 4
  1. Vitali Svetlitchnyi (first)
  2. Christine Peschel (additional)
  3. Georg Acker (additional)
  4. Ortwin Meyer (additional)
References 61 Referenced 189
  1. Acetarin J.-D. Carlemalm E. Villiger W. Development of new Lowicryl resins for embedding biological specimens at even lower temperature.J. Microsc.14319868188 (10.1111/j.1365-2818.1986.tb02766.x) / J. Microsc. / Development of new Lowicryl resins for embedding biological specimens at even lower temperature by Acetarin J.-D. (1986)
  2. Acker G. Immunoelectron microscopy of surface antigens (polysaccharides) of gram-negative bacteria using pre- and post-embedding techniques Electron microscopy in microbiology. Methods in microbiology Mayer F. 20 1988 147 174 Academic Press Ltd. London, England / Electron microscopy in microbiology. Methods in microbiology / Immunoelectron microscopy of surface antigens (polysaccharides) of gram-negative bacteria using pre- and post-embedding techniques by Acker G. (1988)
  3. Albracht S. P. The use of electron-paramagnetic-resonance spectroscopy to establish the properties of nickel and the iron-sulfur cluster in hydrogenase from Chromatium vinosum.Biochem. Soc. Trans.131985582585 (10.1042/bst0130582) / Biochem. Soc. Trans. / The use of electron-paramagnetic-resonance spectroscopy to establish the properties of nickel and the iron-sulfur cluster in hydrogenase from Chromatium vinosum by Albracht S. P. (1985)
  4. Albracht S. P. Hedderich R. Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH-uniquinone oxidoreductase (Complex I).FEBS Lett.485200016 (10.1016/S0014-5793(00)02172-4) / FEBS Lett. / Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH-uniquinone oxidoreductase (Complex I) by Albracht S. P. (2000)
  5. Beisenherz G. Bolze H. J. Bücher T. Czok R. Garbade K. H. Meyer-Arendt E. Pfleiderer G. Diphosphofructose-Aldolase, Phosphoglyceraldehyd-Dehydrogenase, Milchsäure-Dehydrogenase, Glycerophosphat-Dehydrogenase and Pyruvat-Kinase aus Kaninchenmuskulatur in einem Arbeitsgang.Z. Naturforsch. B81953555577 (10.1515/znb-1953-1005) / Z. Naturforsch. B / Diphosphofructose-Aldolase, Phosphoglyceraldehyd-Dehydrogenase, Milchsäure-Dehydrogenase, Glycerophosphat-Dehydrogenase and Pyruvat-Kinase aus Kaninchenmuskulatur in einem Arbeitsgang by Beisenherz G. (1953)
  6. Bonam D. Ludden P. W. Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.J. Biol. Chem.262198729802987 (10.1016/S0021-9258(18)61456-5) / J. Biol. Chem. / Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum by Bonam D. (1987)
  7. 10.1128/jb.159.2.693-699.1984
  8. Bonam D. McKenna M. C. Stephens P. J. Ludden P. W. Nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum: in vivo and in vitro activation by exogenous nickel.Proc. Natl. Acad. Sci. USA8519883135 (10.1073/pnas.85.1.31) / Proc. Natl. Acad. Sci. USA / Nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum: in vivo and in vitro activation by exogenous nickel by Bonam D. (1988)
  9. Bowien B. Meyer F. Codd G. A. Schlegel H. G. Purification, some properties and quaternary structure of the d-ribulose-1,5-diphosphate carboxylase of Alcaligenes eutrophus.Arch. Microbiol.1101976157166 (10.1007/BF00690223) / Arch. Microbiol. / Purification, some properties and quaternary structure of the d-ribulose-1,5-diphosphate carboxylase of Alcaligenes eutrophus by Bowien B. (1976)
  10. 10.1016/0003-2697(76)90527-3
  11. Dawson R. M. C. Elliot D. C. Elliot W. H. Jones K. M. Data for biochemical research. 1986 Oxford University Press Inc New York N.Y
  12. Dobbek H. Gremer L. Meyer O. Huber R. Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcystein.Proc. Natl. Acad. Sci. USA96199988848889 (10.1073/pnas.96.16.8884) / Proc. Natl. Acad. Sci. USA / Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcystein by Dobbek H. (1999)
  13. Drake H. L. Hu S.-I. Wood H. G. Purification of five components from Clostridium thermoaceticum which catalyze synthesis of acetate from pyruvate and methyltetrahydrofolate. Properties of phosphotransacetylase.J. Biol. Chem.25619811113711144 (10.1016/S0021-9258(19)68568-6) / J. Biol. Chem. / Purification of five components from Clostridium thermoaceticum which catalyze synthesis of acetate from pyruvate and methyltetrahydrofolate. Properties of phosphotransacetylase by Drake H. L. (1981)
  14. Ensign S. A. Ludden P. W. Characterization of the CO oxidation/H2 evolution system of Rhodospirillum rubrum: role of a 22-kDa iron-sulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase.J. Biol. Chem.26619911839518403 (10.1016/S0021-9258(18)55283-2) / J. Biol. Chem. / Characterization of the CO oxidation/H2 evolution system of Rhodospirillum rubrum: role of a 22-kDa iron-sulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase by Ensign S. A. (1991)
  15. Ermler U. Grabarse W. Shima S. Goubeaud M. Thauer R. K. Active sites of transition-metal enzymes with a focus on nickel.Curr. Opin. Struct. Biol.81998749758 (10.1016/S0959-440X(98)80095-X) / Curr. Opin. Struct. Biol. / Active sites of transition-metal enzymes with a focus on nickel by Ermler U. (1998)
  16. Ferry J. G. CO dehydrogenase.Annu. Rev. Microbiol.491995305333 (10.1146/annurev.mi.49.100195.001513) / Annu. Rev. Microbiol. / CO dehydrogenase by Ferry J. G. (1995)
  17. Fish W. W. Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples.Methods Enzymol.1581988357364 (10.1016/0076-6879(88)58067-9) / Methods Enzymol. / Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples by Fish W. W. (1988)
  18. Flint D. H. Allen R. M. Iron-sulfur proteins with nonredox functions.Chem. Rev.96199623152334 (10.1021/cr950041r) / Chem. Rev. / Iron-sulfur proteins with nonredox functions by Flint D. H. (1996)
  19. Fogo J. K. Popowsky M. Spectrophotometric determination of hydrogen sulfide.Anal. Chem.211949732734 (10.1021/ac60030a028) / Anal. Chem. / Spectrophotometric determination of hydrogen sulfide by Fogo J. K. (1949)
  20. 10.1128/jb.178.6.1515-1524.1996
  21. 10.1128/jb.178.15.4597-4603.1996
  22. Garcin E. Vernede X. Hatchikian E. C. Volbeda A. Frey M. Fontecilla-Camps J. C. The crystal structure of a reduced [NiFeS] hydrogenase provides an image of the activated catalytic center.Structure71999557566 (10.1016/S0969-2126(99)80072-0) / Structure / The crystal structure of a reduced [NiFeS] hydrogenase provides an image of the activated catalytic center by Garcin E. (1999)
  23. González J. M. Robb F. T. Genetic analysis of Carboxydothermus hydrogenoformans carbon monoxide dehydrogenase genes cooF and cooS.FEMS Microbiol. Lett.1912000243247 (10.1111/j.1574-6968.2000.tb09346.x) / FEMS Microbiol. Lett. / Genetic analysis of Carboxydothermus hydrogenoformans carbon monoxide dehydrogenase genes cooF and cooS by González J. M. (2000)
  24. Gremer L. Meyer O. Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of a molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor.Eur. J. Biochem.2381996862866 (10.1111/j.1432-1033.1996.0862w.x) / Eur. J. Biochem. / Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of a molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor by Gremer L. (1996)
  25. Gremer L. Kellner S. Meyer O. A new type of flavin adenin dinucleotide-binding resolved in the molybdo iron-sulfur-flavoprotein carbon monoxide dehydrogenase from Oligotropha carboxidovorans Flavins and flavoproteins 1999. Ghisla S. Kroneck P. Macheroux P. Sund H. 1999 759 766 Rudolf Weber Agency for Scientific Publications Berlin Germany
  26. Gremer L. Kellner S. Dobbek H. Huber R. Meyer O. Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans.J. Biol. Chem.275200018641872 (10.1074/jbc.275.3.1864) / J. Biol. Chem. / Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans by Gremer L. (2000)
  27. Hänzelmann P. Dobbek H. Gremer L. Huber R. Meyer O. The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.J. Mol. Biol.301200012211235 (10.1006/jmbi.2000.4023) / J. Mol. Biol. / The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase by Hänzelmann P. (2000)
  28. Hänzelmann P. Hofmann B. Meisen S. Meyer O. The redox centers in the molybdo iron-sulfur flavoprotein CO dehydrogenase from the thermophilic carboxidotrophic bacterium Pseudomonas thermocarboxydovorans.FEMS Microbiol. Lett.1761999139145 (10.1111/j.1574-6968.1999.tb13654.x) / FEMS Microbiol. Lett. / The redox centers in the molybdo iron-sulfur flavoprotein CO dehydrogenase from the thermophilic carboxidotrophic bacterium Pseudomonas thermocarboxydovorans by Hänzelmann P. (1999)
  29. Hedderich R. Klimmek O. Kröger A. Dirmeier R. Keller M. Stetter K. O. Anaerobic respiration with elemental sulfur and with disulfides.FEMS Microbiol. Rev.221999353381 (10.1111/j.1574-6976.1998.tb00376.x) / FEMS Microbiol. Rev. / Anaerobic respiration with elemental sulfur and with disulfides by Hedderich R. (1999)
  30. Heo J. Staples C. R. Telser J. Ludden P. W. Rhodospirillum rubrum CO-dehydrogenase. Part 2. Spectroscopic investigation and assignment of spin-spin coupling signals.J. Am. Chem. Soc.12119991104511057 (10.1021/ja990397a) / J. Am. Chem. Soc. / Rhodospirillum rubrum CO-dehydrogenase. Part 2. Spectroscopic investigation and assignment of spin-spin coupling signals by Heo J. (1999)
  31. Heo J. Staples C. R. Halbleib C. M. Ludden P. W. Evidence for a ligand CO that is required for catalytic activity of CO dehydrogenase from Rhodospirillum rubrum.Biochemistry39200079567963 (10.1021/bi992958g) / Biochemistry / Evidence for a ligand CO that is required for catalytic activity of CO dehydrogenase from Rhodospirillum rubrum by Heo J. (2000)
  32. Hu Z. Spangler N. J. Anderson M. E. Xia J. Ludden P. W. Lindahl P. A. Münck E. Nature of the C-cluster in Ni-containing carbon monoxide dehydrogenases.J. Am. Chem. Soc.1181996830845 (10.1021/ja9528386) / J. Am. Chem. Soc. / Nature of the C-cluster in Ni-containing carbon monoxide dehydrogenases by Hu Z. (1996)
  33. 10.1128/jb.171.5.2873-2875.1989
  34. 10.1128/jb.177.8.2241-2244.1995
  35. Kraut M. Hugendieck I. Herwig S. Meyer O. Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria.Arch. Microbiol.1521989335341 (10.1007/BF00425170) / Arch. Microbiol. / Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria by Kraut M. (1989)
  36. Künckel A. Verholt J. A. Thauer R. K. Hedderich R. An Escherichia coli hydrogenase 3-type hydrogenase in methanogenic archaea.Eur. J. Biochem.2521998467476 (10.1046/j.1432-1327.1998.2520467.x) / Eur. J. Biochem. / An Escherichia coli hydrogenase 3-type hydrogenase in methanogenic archaea by Künckel A. (1998)
  37. 10.1038/227680a0
  38. Lax E. D'Ans-Lax: Taschenbuch für Chemiker und Physiker 1 1967 I 1025 Springer Verlag Berlin, Germany / D'Ans-Lax: Taschenbuch für Chemiker und Physiker by Lax E. (1967)
  39. Lundie L. L. Drake H. L. Development of a minimally defined medium for the acetogen Clostridium thermoaceticum.J. Bacteriol.1581984700703 (10.1128/JB.159.2.700-703.1984) / J. Bacteriol. / Development of a minimally defined medium for the acetogen Clostridium thermoaceticum by Lundie L. L. (1984)
  40. Menon A. L. Hendrix H. Hutchins A. Verhagen M. F. J. Adams M. W. W. The δ-subunit of pyruvate ferredoxin oxidoreductase from Pyrococcus furiosus is a redox-active, iron-sulfur protein: evidence for an ancestral relationship with 8Fe-type ferredoxin.Biochemistry3719981283812846 (10.1021/bi980979p) / Biochemistry / The δ-subunit of pyruvate ferredoxin oxidoreductase from Pyrococcus furiosus is a redox-active, iron-sulfur protein: evidence for an ancestral relationship with 8Fe-type ferredoxin by Menon A. L. (1998)
  41. Meuer J. Bartoschek S. Koch J. Künckel A. Hedderich R. Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri.Eur. J. Biochem.2651999325335 (10.1046/j.1432-1327.1999.00738.x) / Eur. J. Biochem. / Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri by Meuer J. (1999)
  42. Meyer O. Frunzke K. Mörsdorf G. Biochemistry of the aerobic utilization of carbon monoxide Microbial growth on C 1 compounds. Murrell J. C. Kelly D. P. 1993 433 459 Intercept Ltd. Andover England
  43. Meyer O. Gremer L. Ferner R. Ferner M. Dobbek H. Gnida M. Meyer-Klaucke W. Huber R. The role of Se, Mo, and Fe in the structure and function of carbon monoxide dehydrogenase.Biol. Chem.3812000865876 (10.1515/BC.2000.108) / Biol. Chem. / The role of Se, Mo, and Fe in the structure and function of carbon monoxide dehydrogenase by Meyer O. (2000)
  44. 10.1007/BF00189635
  45. Ouchterlony Ö. Diffusion-in-gel methods for immunological analysis Progress in allergy Kallos P. Waksman B. VI 1962 30 154 Verlag Karger Basel, Switzerland / Progress in allergy / Diffusion-in-gel methods for immunological analysis by Ouchterlony Ö. (1962)
  46. Pusheva M. A. Sokolova T. G. Gerhardt M. Svetlichnyi V. A. Hydrogenase, formate dehydrogenase and CO dehydrogenase activities of the thermophilic anaerobic carboxydotrophic bacterium Carboxydothermus hydrogenoformans strain Z-2906.Mikrobiologiya611992939944 / Mikrobiologiya / Hydrogenase, formate dehydrogenase and CO dehydrogenase activities of the thermophilic anaerobic carboxydotrophic bacterium Carboxydothermus hydrogenoformans strain Z-2906 by Pusheva M. A. (1992)
  47. Ragsdale S. W. Kumar M. Nickel-containing carbon monoxide dehydrogenase/acetyl-CoA synthase.Chem. Rev.96199625152539 (10.1021/cr950058+) / Chem. Rev. / Nickel-containing carbon monoxide dehydrogenase/acetyl-CoA synthase by Ragsdale S. W. (1996)
  48. 10.1128/jb.155.3.1224-1237.1983
  49. Raybuck S. A. Bastian N. R. Orme-Johnson W. H. Walsh C. T. Kinetic characterization of the carbon monoxide-acetyl-CoA (carbonyl group) exchange activity of the acetyl-CoA synthesizing CO dehydrogenase from Clostridium thermoaceticum.Biochemistry27198876987702 (10.1021/bi00420a019) / Biochemistry / Kinetic characterization of the carbon monoxide-acetyl-CoA (carbonyl group) exchange activity of the acetyl-CoA synthesizing CO dehydrogenase from Clostridium thermoaceticum by Raybuck S. A. (1988)
  50. Rohde M. Mayer F. Meyer O. Immunocytochemical localization of carbon monoxide oxidase in Pseudomonas carboxydovorans. The enzyme is attached to the inner aspect of the cytoplasmic membrane.J. Biol. Chem.25919841478814792 (10.1016/S0021-9258(17)42672-X) / J. Biol. Chem. / Immunocytochemical localization of carbon monoxide oxidase in Pseudomonas carboxydovorans. The enzyme is attached to the inner aspect of the cytoplasmic membrane by Rohde M. (1984)
  51. Rohde M. Gerberding H. Mund T. Kohring G.-W. Immunoelectron microscopic localization of bacterial enzymes: pre- and post-embedding labelling techniques on resin-embedded samples Electron microscopy in microbiology. Methods in microbiology Mayer F. 20 1988 175 210 Academic Press Ltd. London, England / Electron microscopy in microbiology. Methods in microbiology / Immunoelectron microscopic localization of bacterial enzymes: pre- and post-embedding labelling techniques on resin-embedded samples by Rohde M. (1988)
  52. Sokolova T. G. Gonzáles J. M. Kostrikina N. A. Chernyh N. A. Tourova T. P. Kato C. Bonch-Osmolovskaya E. A. Robb F. T. Carboxydobrachium pacificum gen. nov., sp. nov., a new anaerobic, thermophilic, CO-utilizing bacterium from Okinawa Trough.Int. J. Syst. Evol. Microbiol.512001141149 (10.1099/00207713-51-1-141) / Int. J. Syst. Evol. Microbiol. / Carboxydobrachium pacificum gen. nov., sp. nov., a new anaerobic, thermophilic, CO-utilizing bacterium from Okinawa Trough by Sokolova T. G. (2001)
  53. Staples C. R. Heo J. Spangler N. J. Kerby R. L. Roberts G. P. Ludden P. W. Rhodospirillum rubrum CO-dehydrogenase. Part I. Spectroscopic studies of CODH variant C531A indicate the presence of a binuclear [FeNi] cluster.J. Am. Chem. Soc.12119991103411044 (10.1021/ja990396i) / J. Am. Chem. Soc. / Rhodospirillum rubrum CO-dehydrogenase. Part I. Spectroscopic studies of CODH variant C531A indicate the presence of a binuclear [FeNi] cluster by Staples C. R. (1999)
  54. Svetlichny V. A. Sokolova T. G. Gerhardt M. Kostrikina N. A. Zavarzin G. A. Anaerobic extremely thermophilic carboxydotrophic bacteria in hydrotherms of Kuril Islands.Microb. Ecol.211991110 (10.1007/BF02539140) / Microb. Ecol. / Anaerobic extremely thermophilic carboxydotrophic bacteria in hydrotherms of Kuril Islands by Svetlichny V. A. (1991)
  55. Svetlichny V. A. Sokolova T. G. Gerhardt M. Ringpfeil M. Kostrikina N. A. Zavarzin G. A. Carboxydothermus hydrogenoformans gen. nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hydrothermal environments of Kunashir island.Syst. Appl. Microbiol.141991254260 (10.1016/S0723-2020(11)80377-2) / Syst. Appl. Microbiol. / Carboxydothermus hydrogenoformans gen. nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hydrothermal environments of Kunashir island by Svetlichny V. A. (1991)
  56. Svetlichny V. A. Sokolova T. G. Kostrikina N. A. Lysenko A. M. A new thermophilic anaerobic carboxydotrophic bacterium Carboxydothermus restrictus sp. nov.Mikrobiologiya631994294297 / Mikrobiologiya / A new thermophilic anaerobic carboxydotrophic bacterium Carboxydothermus restrictus sp. nov by Svetlichny V. A. (1994)
  57. Terlesky K. C. Ferry J. G. Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetate-grown Methanosarcina thermophila.J. Biol. Chem.263198840754079 (10.1016/S0021-9258(18)68892-1) / J. Biol. Chem. / Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetate-grown Methanosarcina thermophila by Terlesky K. C. (1988)
  58. Uffen R. L. Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate.Proc. Natl. Acad. Sci. USA73197632983302 (10.1073/pnas.73.9.3298) / Proc. Natl. Acad. Sci. USA / Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate by Uffen R. L. (1976)
  59. 10.1128/jb.155.3.956-965.1983
  60. Volbeda A. Charon M.-H. Piras C. Hatchikian E. C. Frey M. Fontecilla-Camps J. C. Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.Nature3731995580587 (10.1038/373580a0) / Nature / Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas by Volbeda A. (1995)
  61. Wolin E. A. Wolin M. J. Wolfe R. S. Formation of methane by bacterial extracts.J. Biol. Chem.238196322822286 (10.1016/S0021-9258(18)67912-8) / J. Biol. Chem. / Formation of methane by bacterial extracts by Wolin E. A. (1963)
Dates
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Created 23 years, 1 month ago (July 27, 2002, 6:01 a.m.)
Deposited 4 years, 1 month ago (July 29, 2021, 1:59 p.m.)
Indexed 3 days, 13 hours ago (Aug. 31, 2025, 6:30 a.m.)
Issued 24 years ago (Sept. 1, 2001)
Published 24 years ago (Sept. 1, 2001)
Published Print 24 years ago (Sept. 1, 2001)
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@article{Svetlitchnyi_2001, title={Two Membrane-Associated NiFeS-Carbon Monoxide Dehydrogenases from the Anaerobic Carbon-Monoxide-Utilizing Eubacterium Carboxydothermus hydrogenoformans}, volume={183}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.183.17.5134-5144.2001}, DOI={10.1128/jb.183.17.5134-5144.2001}, number={17}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Svetlitchnyi, Vitali and Peschel, Christine and Acker, Georg and Meyer, Ortwin}, year={2001}, month=sep, pages={5134–5144} }