The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites

Vera G Grivennikova, Robert Roth, Natalia V Zakharova, Cecilia Hägerhäll, Andrei D Vinogradov

Research output: Contribution to journalArticlepeer-review

40 Citations (SciVal)

Abstract

The catalytic properties of the rotenone-sensitive NADH:ubiquinone reductase (Complex I) in bovine heart submitochondrial particles and in inside-out vesicles derived from Paracoccus denitrificans and Rhodobacter capsulatus were compared. The prokaryotic enzymes catalyze the NADH oxidase and NADH:quinone reductase reactions with similar kinetic parameters as those for the mammalian Complex I, except for lower apparent affinities for the substrates-nucleotides. Unidirectional competitive inhibition of NADH oxidation by ADP-ribose, previously discovered for submitochondrial particles, was also evident for tightly coupled P. denitrificans vesicles, thus suggesting that a second, NAD+-specific site is present in the simpler prokaryotic enzyme. The inhibitor sensitivity of the forward and reverse electron transfer reactions was compared. In P. denitrificans and Bos taurus vesicles different sensitivities to rotenone and Triton X-100 for the forward and reverse electron transfer reactions were found. In bovine heart preparations, both reactions showed the same sensitivity to piericidin, and the inhibition was titrated as a straight line. In P. denitrificans, the forward and reverse reactions show different sensitivity to piericidin and the titrations of both activities were curvilinear with apparent I50 (expressed as mole of inhibitor per mole of enzyme) independent of the enzyme concentration. This behavior is explained by a model involving two different sites rapidly interacting with piericidin within the hydrophobic phase.
Original languageEnglish
Pages (from-to)79-90
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1607
Issue number2-3
DOIs
Publication statusPublished - 2003

Subject classification (UKÄ)

  • Biological Sciences

Keywords

  • Tightly bound inhibitor
  • NADH:ubiquinone reductase
  • Complex I
  • NDH-1
  • Ubiquinone
  • Piericidin
  • Bovine heart submitochondrial particle
  • Paracoccus denitrificans membrane
  • Rhodobacter capsulatus membrane
  • Respiratory chain

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