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NADH-linked fumarate reductase and NADH dehydrogenase activities inFibrobacter succinogenes

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Abstract

Crude membrane preparation fromFibrobacter succinogenes S85 were investigated and found to contain NADH dehydrogenase (NADH:decylubiquinone oxidoreductase) and NADH-linked fumarate reductase activities. Under aerobic conditions the maximum NADH dehydrogenase activity (252 nmoles/min/mg protein) was ten times greater than that of NADH-fumarate reductase (23 nmoles/min/mg protein). NADH-fumarate reductase was strongly inhibited by 2-heptyl-4-hydroxyquinoline-N-oxide (HOQNO), rotenone, HgCl2, ando-phenanthroline. Inhibition of the NADH dehydrogenase by the first three compounds, particularly rotenone, accounted for most of the effects on NADH-fumarate reductase. The α-band of ab-type cytochrome was resolved into two cytochromes, a cytochromeb 560 (oxidized by addition of HOQNO) and a cytochromeb 563 (oxidized by subsequent addition of fumarate).

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Literature Cited

  1. Deeb SS, Hagen LP (1964) Crystalline cytochrome b1 fromEscherichia coli. J Biol Chem 239:1024–1031

    Google Scholar 

  2. Joyner AE, Baldwin RL (1966) Enzymatic studies of pure cultures of rumen microorganisms. J Bacteriol 92:1321–1330

    Google Scholar 

  3. Matsushita K, Ohnishi T, Kaback HR (1987) NADH-ubiquinone oxidoreductases ofEscherichia coli aerobic respiratory chain. Biochemistry 25:2321–2327

    Google Scholar 

  4. Meinhardt SW, Matsushita K, Kaback HR, Ohnishi T (1989) EPR characterization of the iron-sulfur-containing NADH-ubiquinone oxidoreductase ofEscherichia coli aerobic respiratory chain. Biochemistry 28:2153–2160.

    Google Scholar 

  5. Meinhardt SW, Wang DC, Hon-nami K, Yagi T, Oshima T, Ohnishi T (1990) Studies on the NADH-menaquinone oxidore-ductase segment of the respiratory chain ofThermus thermophilus HB-8. J Biol Chem 265:1360–1368

    Google Scholar 

  6. Miller TL (1978) The pathway of formation of acetate and succinate from pyruvate byBacteroides succinogenes. Arch Microbiol 117:145–152

    Google Scholar 

  7. Miller TL, Wolin MJ (1974) A serum bottle modification of the Hungate technique for cultivating obligate anaerobes. Appl Microbiol 27:985–987

    Google Scholar 

  8. Mountfort DO, Roberton AM (1977) The role of menaquinone and b-type cytochrome in anaerobic reduction of fumarate by NADH in membrane preparations fromBacteroides ruminicola strain B14. J Gen Microbiol 100:309–317

    Google Scholar 

  9. Ohinishi T, Meinhardt SW, Matsushita K, Kaback HR (1987) The NADH-UQ oxidoreductase system ofEscherichia coli. In: Ozawa T, Papa S (eds) Bioenergetics: structure and function of energy transducing systems. Tokyo, Berlin: Japan Sci Soc Press, Springer-Verlag, pp 19–29

    Google Scholar 

  10. Reddy CA (1967) Studies on DNA base composition and chtochromes in certain species of the genusBacteroides. MS Thesis, University of Illinois, Urbana, Ill., USA

    Google Scholar 

  11. Schwartz AC, Sporkenbach J (1975) The electron transport system of the anaerobicPropionibacterium shermanii. Cytochrome and inhibitor studies. Arch Microbiol 102:261–273

    Google Scholar 

  12. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC (1985) Measurement of protein using bicinchoninic acid. Anal Biochem 150:76–85

    Google Scholar 

  13. Stewart CS, Flint HJ (1989)Bacteroides (Fibrobacter) succinogenes, a cellulolytic anaerobic bacterium from the gastrointestinal tract. Appl Microbiol Biotechnol 30:433–439

    Google Scholar 

  14. Thauer RK, Jungermann K, Decker K (1977) Energy conservation in chemotrophic anaerobic bacteria. Bacteriol Rev 41:100–180

    Google Scholar 

  15. van Verseveld HW, Boon JP, Stouthamer AH (1979) Growth yields and the efficiency of oxidative phosphorylation ofParacoccus denitrificans during two-(carbon) substrate-limited growth. Arch Microbiol 121:213–223

    Google Scholar 

  16. Watkins WE, Glass TL (1991) Characteristics of 16-dehydroprogesterone reductase in cell extracts of the intestinal anaerobe,Eubacterium sp. strain 144. J Steroid Biochem Molec Biol 38:257–263

    Google Scholar 

  17. Yagi T (1987) Inhibition of NADH-ubiquinone reductase activity by N,N′-dicyclohexylcarbodiimide and correlation of this inhibition with the occurrence of energy coupling site 1 in various organisms. Biochemistry 26:2822–2828

    Google Scholar 

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Authors and Affiliations

  1. Department of Biochemistry, North Dakota State University Fargo, North Dakota, USA

    Steven W. Meinhardt

  2. Department of Veterinary and Microbiological Sciences, North Dakota State University Fargo, 58105, North Dakota, USA

    Thomas L. Glass

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  1. Steven W. Meinhardt
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  2. Thomas L. Glass
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Published with the approval of the Director of the Agricultural Experiment Station, North Dakota State University, as journal article no. 2137.

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Meinhardt, S.W., Glass, T.L. NADH-linked fumarate reductase and NADH dehydrogenase activities inFibrobacter succinogenes . Current Microbiology 28, 247–251 (1994). https://doi.org/10.1007/BF01575969

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  • DOI: https://doi.org/10.1007/BF01575969

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