Zusammenfassung
In zellfreien Extrakten aus Hydrogenomonas H 16 ist die Hydrogenase-Aktivität auf zwei Fraktionen verteilt, die durch einstündiges Zentrifugieren bei 100 000 g voneinander getrennt werden können. Die überstehende Fraktion reduziert Methylenblau, NAD, FMN, FAD und Sauerstoff, aber nicht NADP. Die Partikelfraktion reduziert Methylenblau und, anscheinend als einzigen physiologischen H-Acceptor, Sauerstoff. Cyanid und Kohlenmonoxyd hemmen nur die Sauerstoff-Reduktion durch die Partikelfraktion, aber nicht die der überstehenden Fraktion. Die Funktionen der beiden Hydrogenasen werden diskutiert.
Summary
In cell-free extracts of Hydrogenomonas H 16, the hydrogenase activity is found in two fractions which can be separated by centrifugation at 100000 g for one hour. The supernatant reduces methylene blue, NAD, FMN, FAD and oxygen, but not NADP. The particle fraction reduces methylene blue and apparently, only oxygen as a physiological H-acceptor. Cyanide and carbon monoxide inhibit oxygen reduction by the particle fraction, but not that of the supernatant. The functions of both hydrogenases are discussed.
Literatur
Ahrens, J.: persönliche Mitteilung 1965.
Akagi, J. M., and L. L. Campbell: Studies on thermophilic sulfatereducing bacteria. II. Hydrogenase activity of Clostridium nitrificans. J. Bact. 82, 927 (1961).
Asnis, R. G., V. G. Vely, and M. C. Glick: Some enzymatic activities of particulate fraction from sonic lysates of Escherichia coli. J. Bact. 72, 314 (1956).
Atkinson, D. E.: Hydrogen metabolism in Acetobacter peroxidans. J. Bact. 72, 189 (1956).
—, and B. McFadden: The biochemistry of Hydrogenomonas. I. The hydrogenase of Hydrogenomonas facilis in cell-free preparations. J. biol. Chem. 210, 885 (1954).
Bartha, R.: Physiologische Untersuchungen über den chemolithotrophen Stoffwechsel neu isolierter Hydrogenomonas-Stämme. Arch. Mikrobiol. 41, 313 (1962).
Bernstein, S., and W. Vishniao: Purification and properties of a DPN-linked hydrogenase. Fed. Proc. 18, 192 (1958).
Bone, D. H.: Localization of hydrogen activating enzymes in Pseudomonas saccharophila. Biochem. biophys. Res. Commun. 3, 211 (1960).
—, and W. Vishniac: Purification and properties of different forms of hydrogen dehydrogenase. Biochim. biophys. Acta (Amst.) 67, 581 (1963).
Bose, S. K., and H. Gest: Hydrogenase and light-stimulated electron transfer reactions in photosynthetic bacteria. Nature (Lond.) 195, 1168 (1962).
Cota-Robles, E. H., A. G. Marr, and E. H. Nilson: Submicroscopic particles in extracts of Azotobacter vinelandii. J. Bact. 72, 243 (1958).
Dolin, M. I.: Cytochrome-independent electron transport enzymes in bacteria. In: I. C. Gunsalus and R. Y. Stanier: The bacteria II, p. 425, New York: Academic Press 1961.
Eberhardt, U.: Die Anreicherung von Knallgasbakterien. In: Anreicherungskultur und Mutantenauslese. Zbl. Bakt., I. Abt. Orig. Suppl. 1, 155 (1965).
Fredricks, W. W., and E. R. Stadtman: The role of ferredoxin in the hydrogenase system from Clostridium kluyveri. J. biol. Chem. 240, 4065 (1965).
Gest, H.: Molecular hydrogen: oxidation and formation in cellfree systems. In: W. D. McElroy and B. Glass; Phosphorus metabolism II, p. 522, Baltimore: The Johns Hopkins Press 1952a.
—: The properties of cell-free hydrogenases of Escherichia coli and Rhodospirillum rubrum. J. Bact. 63, 111 (1952b).
Gottschalk, G.: Die Biosynthese der Poly-β-hydroxybuttersäure durch Knallgasbakterien. Diss., Göttingen 1963.
Hughes, D. E.: A press for disrupting bacteria and other microorganisms. Brit. J. exp. Path. 32, 97 (1951).
Hyndman, L. A., R. H. Burris, and P. W. Wilson: Properties of hydrogenase from Azotobacter vinelandii. J. Bact. 65, 522 (1953).
King, N. K., and M. E. Winfield: The assay of soluble hydrogenase. Biochim. biophys. Acta (Amst.) 18, 431 (1955).
Kinsky, S. C., E. R. Stadtman, and M. K. MacClay: Cofactor requirements for the pyridine nucleotide reduction by hydrogen. J. biol. Chem. 236, 574 (1960).
Krasna, A. I., E. Riklis, and D. Rittenberg: The purification and properties of the hydrogenase of Desulfovibrio desulfuricans. J. biol. Chem. 235, 2717 (1960).
La Riviere, J. W. M.: On the microbial metabolism of the tartaric acid isomeres. Diss., Delft 1958.
Lascelles, J.: Electron transport structures. In M. R. Pollock and M. H. Richmond, ed.: Function and structure in microorganisms, 15th Symp. Soc. Gen. Microbiol., p. 32. Cambridge: University Press 1965.
Milner, H. W., N. S. Lawrence, and C. S. French: Colloidal dispersion of chloroplast material. Science 111, 633 (1950).
Packer, L.: Respiratory carriers involved in the oxidation of hydrogen and lactate in facultative autotroph. Arch. Biochem. 78, 54 (1958).
—, and W. Vishniac: The specifity of a diphosphopyridine nucleotide linked hydrogenase. Biochim. biophys. Acta (Amst.) 17, 153 (1955).
Repaske, R.: The electron transport system of Hydrogenomonas eutropha. I. Diphosphopyridine nucleotide reduction by hydrogen. J. biol. Chem. 237, 1351 (1962).
—, and C. Seward: FMN as a cofactor in the enzymatic reduction of DPN by hydrogen. Biochem. biophys. Res. Commun. 2, 397 (1960).
Rose, I. A., and S. Ochoa: Phosphorylation by particulate preparations of Azotobacter vinelandii. J. biol. Chem. 220, 307 (1956).
Sadana, J. C., and A. V. Jagannathan: Purification and properties of the hydrogenase of Desulfovibrio desulfuricans. Biochim. biophys. Acta (Amst.) 19, 440 (1956).
—, and A. V. Morey: Purification and properties of the hydrogenase of Desulfovibrio desulfuricans. Biochim. biophys. Acta (Amst.) 50, 153 (1961).
San Pietro, A.: Assay and properties of hydrogenases. In S. P. Colowick and N. O. Kaplan: Methods in enzymology II, p. 861. New York: Academic Press 1955.
Schindler, J.: Die Synthese von Poly-β-hydroxybuttersäure durch Hydrogenomonas H 16: Die zu β-Hydroxybutyryl-Coenzym A führenden Reaktionsschritte. Diss., Göttingen 1964.
Schlegel, H. G., H. Kaltwasser u. G. Gottschalk: Ein Submersverfahren zur Kultur wasserstoffoxydierender Bakterien: Wachstumsphysiologische Untersuchungen. Arch. Mikrobiol. 38, 209 (1961a).
— u. R. Stellmach-Helwig: Quantitative Messungen über den CO2-Einbau an organotrophen Bakterien. Arch. Mikrobiol. 38, 55 (1961b).
Schmidt, K., S. Liaaen Jensen u. H. G. Schlegel: Die Carotinoide der Thiorhodaceae. I. Okenon als Hauptcarotinoid von chromatium okenii Perty. Arch. Mikrobiol. 46, 117 (1963).
Shug, A. L., P. B. Hamilton, and P. W. Wilson: Hydrogen and nitrogen fixation. In W. D. McElroy and B. Glass: Inorganic nitrogen metabolism, p. 344. Baltimore: The Johns Hopkins Press 1956.
Tanenbaum, S. W.: The metabolism of Acetobacter peroxidans. II. Hydrogen activating and related enzymes. Biochim. biophys. Acta (Amst.) 21, 343 (1956).
Vishniac, W., and P. A. Trudinger: Carbon dioxide fixation and substrate oxidation in chemosynthetic sulfur and hydrogen bacteria. In: Symposium on Autotrophy. Bact. Rev. 26, 168 (1962).
Wilde, E.: Untersuchungen über Wachstum und Speicherstoffsynthese von Hydrogenomonas. Arch. Mikrobiol. 43, 109 (1962).
Wittenberger, C. L. and R. Repaske: Studies on hydrogen oxidation in cell-free extracts of Hydrogenomonas eutropha. Biochim. biophys. Acta (Amst.) 47, 542 (1961).
Author information
Authors and Affiliations
Additional information
Auszug aus der gleichlautenden Dissertation der mathematisch-naturwissen-schaftlichen Fakultät der Universität Göttingen 1965.
Rights and permissions
About this article
Cite this article
Eberhardt, U. Über das Wasserstoff aktivierende System von Hydrogenomonas H16. Archiv. Mikrobiol. 53, 288–302 (1966). https://doi.org/10.1007/BF00446675
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00446675