Archives of Microbiology

, Volume 102, Issue 1, pp 261–273 | Cite as

The electron transport system of the anaerobic Propionibacterium shermanii

Cytochrome and inhibitor studies
  • Arnold C. Schwartz
  • Jutta Sporkenbach
Short Communications
Received:

Abstract

  1. 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. 2.

    Spectral investigation of the electron transport particles revealed the presence of cytochromes b, d and o, and traces of cytochrome a1 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. 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. 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. 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. 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.

     

Key words

Propionibacterium shermanii Anaerobic Electron Transport Electron Transport Particles Cytochromes Menaquinone Fumarate Reductase Site of NQNO Inhibition 

Unusual 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

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Copyright information

© Springer-Verlag 1975

Authors and Affiliations

  • Arnold C. Schwartz
    • 1
  • Jutta Sporkenbach
    • 1
  1. 1.Botanisches Institut der Universität BonnBonnGermany

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