Archives of Microbiology

, Volume 139, Issue 4, pp 332–337 | Cite as

Functional relationship between protein-bound and free factor F430 in Methanobacterium

  • Dorothe Ankel-Fuchs
  • Rolf Jaenchen
  • Norbert A. Gebhardt
  • Rudolf K. Thauer
Original Papers


Factor F430 is a nickel porphinoid present in all methanogenic bacteria. It is a component of methyl-CoM reductase to which it is tightly but not covalently bound. Evidence is presented that in Methanobacterium thermoautotrophicum grown on nickel sufficient medium only approximately 30% of total F430 is associated with methyl-CoM reductase and that 70% is present in a non-bound, free form. When such cells were transferred to a nickel deficient medium the bacteria continued to grow although synthesis of total F430 stopped. During growth in the absence of nickel the amount of total F430 per 1 culture remained constant and that per g cells decreased. The ratio of free F430 to bound F430, however, changed. Free F430 was converted into the protein-bound form until almost all of the free F430 had disappeared. The kinetics of labelling with 63Ni of free and bound F430 agreed rather well with that calculated for a precursor-product relationship between free and bound F430.

Key words

Factor F430 Coenzyme F430 Nickel porphinoid Tetrapyrroles Methyl-CoM reductase Methanogenic bacteria Methanobacterium thermoautotrophicum 


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Copyright information

© Springer-Verlag 1984

Authors and Affiliations

  • Dorothe Ankel-Fuchs
    • 1
  • Rolf Jaenchen
    • 1
  • Norbert A. Gebhardt
    • 1
  • Rudolf K. Thauer
    • 1
  1. 1.Fachbereich Biologie, MikrobiologiePhilipps-UniversitätMarburgFederal Republic of Germany

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