Abstract
-
1.
Electron transport particles obtained from cellfree extracts of Propionibacterium shermanii by centrifugation at 105000xg for 3 hrs oxidized NADH, d,l-lactate, l-glycerol-3-phosphate and succinate with oxygen and, except for succinate, with fumarate, too.
-
2.
Spectral investigation of the electron transport particles revealed the presence of cytochromes b, d and o, and traces of cytochrome a 1 and a c-type cytochrome. Cytochrome b was reduced by succinate to about 50%, and by NADH, lactate or glycerol-3-phosphate to 80–90.
-
3.
The inhibitory effects of amytal and rotenone on NADH oxidation, but not on the oxidation of the other substrates, indicated the presence of the NADH dehydrogenase complex, or “site I region”, in the electron transport system of P. shermanii.
-
4.
NQNO inhibited substrate oxidations by oxygen and fumarate, as well as equilibration of the flavoproteins of the substrate dehydrogenases by way of menaquinone. The inhibition occurred at low concentrations of the inhibitor, and reached 80–100%, depending on the substrate tested. The site of inhibition of the respiratory activity was located between menaquinone and cytochrome b. In addition, inhibition of flavoprotein equilibration suggested that NQNO acted upon the electron transfer directed from menaquinol towards the acceptor to be reduced, either cytochrome b or the flavoproteins, which would include fumarate reductase.
-
5.
In NQNO-inhibited particles, cytochrome b was not oxidized by oxygen-free fumarate, but readily oxidized by oxygen. It was concluded from this and the above evidence that the branching-point of the electron transport chain towards fumarate reductase was located at the menaquinone in P. shermanii. It was further concluded that all cytochromes were situated in the oxygen-linked branch of the chain, which formed a dead end of the system under anaerobic conditions.
-
6.
Antimycin A inhibited only oxygen-linked reactions of the particles to about 50% at high concentrations of the inhibitor. Inhibitors of terminal oxidases were inactive, except for carbon monoxide.
Article PDF
Avoid common mistakes on your manuscript.
Abbreviations
- ET:
-
electron transport
- G-3-P:
-
glycerol-3-phosphate
- NQNO:
-
2-n-nonyl-4-hydroxyquinoline-N-oxide
- PMS:
-
phenazine methosulfate
- TMPD:
-
tetramethyl-p-phenylene diamine
References
Bauchop, T., Elsden, S.R.: The growth of microorganisms in relation to their energy supply. J. gen. Microbiol. 23, 457–469 (1960)
Bonartzeva, G.A., Taptykova, S.D., Vorobieva, L.I., Krainova, O.A., Briukhacheva, N.L.: Aerobic metabolism of propionic bacteria. Mikrobiologiya 42, 765–771 (1973)
Brodie, A.F.: The role of naphthoquinones in oxidative metabolism. In: Biochemistry of quinones, R. A. Morton, ed., pp. 355–404. London-New York:Academic Press 1965
Castor, L.N., Chance, B.: Photochemical determination of the oxidases of bacteria. J. biol. Chem. 234, 1587–1592 (1959)
Chaix, P., Fromageot, C.: Les cytochromes de Propionibacterium pentosaceum. Trav. des membres de la Soc. Chim. Biol. (France) 24, 1125–1127 (1942)
Chance, B.: Spectra and reaction kinetics of respiratory pigments of homogenized and intact cells. Nature (Lond.) 169, 215–221 (1952)
Chance, B.: The kinetics and inhibition of cytochrome components of the succinic oxidase system. III. Cytochrome b. J. biol. Chem. 233, 1223–1229 (1958)
Chance, B., Williams, G.R.: Respiratory enzymes in oxidative phosphorylation. II. Difference spectra. J. biol. Chem. 217, 395–407 (1955)
Cornforth, J.W., James, A.T.: Structure of a naturally occurring antagonist of dihydrostreptomycin. Biochem. J. 63, 124–130 (1956)
Cox, G.B., Newton, N.A., Gibson, F., Snoswell, A.M., Hamilton, J.A.: The function of ubiquinone in Escherichia coli. Biochem. J. 117, 551–562 (1970)
Daniel, R.M.: The electron transport system of Acetobacter suboxydans with particular reference to cytochrome o. Biochim. biophys. Acta (Amst.) 216, 328–341 (1970)
Deeb, S.S., Hager, L.P.: Crystalline cytochrome b 1 from Escherichia coli. J. biol. Chem. 239, 1024–1031 (1964)
DeVries, W., van Wyck-Kapteyn, W.M.C., Stouthamer, A.H.: Influence of oxygen on growth, cytochrome synthesis and fermentation pattern in propionic acid bacteria. J. gen. Microbiol. 71, 515–524 (1972)
DeVries, W., van Wyck-Kapteyn, W.M.C., Stouthamer, A.H.: Generation of ATP during cytochrome-linked anaerobic electron transport in propionic acid bacteria. J. gen. Microbiol. 76, 31–41 (1973)
Ernster, L., Lee, I.-Y., Norling, B., Persson, B.: Studies with ubiquinone-depleted submitochondrial particles. Essentiality of ubiquinone for the interaction of succinate dehydrogenase, NADH dehydrogenase, and cytochrome b. Europ. J. Biochem. 9, 299–310 (1969)
Estabrook, R.W.: Mitochondrial respiratory control and the polarographic measurement of ADP: O ratios. In: Methods in enzymology, Vol. X, R. W. Estabrook, M. E. Pullmann, eds., pp. 41–47. New York-London: Academic Press 1967
Hatchikian, E.C.: On the role of menaquinone-6 in the electron transport of hydrogen:fumarate reductase system in the strict anaerobe Desulfovibrio gigas. J. gen. Microbiol. 81, 261–266 (1974)
Hatchikian, E.C., LeGall, J.: Evidence for the presence of a b-type cytochrome in the sulfate reducing bacterium Desulfovibrio gigas, and its role in the reduction of fumarate by molecular hydrogen. Biochim. biophys. Acta (Amst.) 267, 479–484 (1972)
Kamen, M.D., Horio, T.: Bacterial cytochromes. I. Structural aspects. Ann. Rev. Biochem. 39, 673–700 (1970)
Kröger, A., Dadak, V.: On the role of quinones in bacterial electron transport. The respiratory system of Bacillus megaterium. Europ. J. Biochem. 11, 328–340 (1969)
Kröger, A., Dadak, V., Klingenberg, M., Diemer, F.: On the role of quinones in bacterial electron transport. Differential roles of ubiquinone and menaquinone in Proteus rettgeri. Europ. J. Biochem. 21, 322–333 (1971)
Kröger, A., Klingenberg, M.: On the role of ubiquinone in mitochondria. II. Redox reactions of ubiquinone in the control of oxidative phosphorylation. Biochem. Z. 344, 317–336 (1966)
Kröger, A., Klingenberg, M.: The kinetics of the redox reactions of ubiquinone related to the electron transport activity in the respiratory chain. Europ. J. Biochem. 34, 358–368 (1973a)
Kröger, A., Klingenberg, M.: Further evidence for the pool function of ubiquinone as derived from the inhibition of the electron transport by antimycin. Europ. J. Biochem. 39, 313–323 (1973b)
Kurup, C.K.R., Brodie, A.F.: Oxidative phosphorylation in fractionated bacterial systems. XXV. Studies on the involvement of metal in Mycobacterium phlei. J. biol. Chem. 242, 197–203 (1967)
Lara, F.J.S.: The succinic dehydrogenase of Propionibacterium pentosaceum. Biochim. biophys. Acta (Amst.) 33, 565–567 (1959)
Lightbown, J.W., Jackson, F.L.: Inhibition of cytochrome systems of heart muscle and certain bacteria by the antagonists of dihydrostreptomycin: 2-alkyl-4-hydroxyquinoline N-oxides. Biochem. J. 63, 130–137 (1956)
Ohnishi, T.: Mechanism of electron transport and energy conservation in the site I region of the respiratory chain. Biochim. biophys. Acta (Amst.) 301, 105–128 (1973)
Schwartz, A.C.: Zur Wirkung des Sauerstoffs auf ruhende Zellen von Propionibacterium shermanii. In: 2. Symposium Technische Mikrobiologie, H. Dellweg, ed., pp. 175–182. Berlin: Institut für Gärungsgewerbe und Biotechnologie 1970
Schwartz, A.C.: A natural menaquinone participating in the electron transport system of the anaerobic Propionibacterium shermanii. Abstr. Commun. Meet. Fed. Eur. Biochem. Soc. 8, no. 1089 (1972)
Schwartz, A.C.: Terpenoid quinones of the anaerobic Propionibacterium shermanii. I. (II, III)-tetrahydromenaquinone-9. Arch. Mikrobiol. 91, 273–279 (1973a)
Schwartz, A.C.: Anaerobiosis and oxygen consumption of some strains of Propionibacterium and a modified method for comparing the oxygen sensitivity of various anaerobes. Z. allg. Mikrobiol. 13, 681–691 (1973b)
Sone, N.: The redox reactions in propionic acid fermentasystem I. Occurrence and nature of an electron transfer system in Propionibacterium arabinosum. J. Biochem. (Jap.) 71, 931–940 (1972)
Yamanaka, T., Okunuki, K.: Crystalline Pseudomonas cytochrome oxidase. I. Enzymic properties with special reference to the biological specificity. Biochim. biophys. Acta (Amst.) 67, 379–393 (1963)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Schwartz, A.C., Sporkenbach, J. The electron transport system of the anaerobic Propionibacterium shermanii . Arch. Microbiol. 102, 261–273 (1975). https://doi.org/10.1007/BF00428377
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00428377