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

Grivennikova, Vera G; Roth, Robert LU ; Zakharova, Natalia V; Hägerhäll, Cecilia LU and Vinogradov, Andrei D (2003) In Biochimica et Biophysica Acta - Bioenergetics 1607(2-3). p.79-90
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.... (More)
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. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
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
in
Biochimica et Biophysica Acta - Bioenergetics
volume
1607
issue
2-3
pages
79 - 90
publisher
Elsevier
external identifiers
  • pmid:14670598
  • wos:000187241500002
  • scopus:0345059204
ISSN
0005-2728
DOI
10.1016/j.bbabio.2003.09.001
language
English
LU publication?
yes
id
c7126095-0f1e-466d-b20f-0ba4d49fd728 (old id 124620)
date added to LUP
2007-07-04 17:29:03
date last changed
2018-06-24 04:42:43
@article{c7126095-0f1e-466d-b20f-0ba4d49fd728,
  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.},
  author       = {Grivennikova, Vera G and Roth, Robert and Zakharova, Natalia V and Hägerhäll, Cecilia and Vinogradov, Andrei D},
  issn         = {0005-2728},
  keyword      = {Tightly bound inhibitor,NADH:ubiquinone reductase,Complex I,NDH-1,Ubiquinone,Piericidin,Bovine heart submitochondrial particle,Paracoccus denitrificans membrane,Rhodobacter capsulatus membrane,Respiratory chain},
  language     = {eng},
  number       = {2-3},
  pages        = {79--90},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta - Bioenergetics},
  title        = {The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites},
  url          = {http://dx.doi.org/10.1016/j.bbabio.2003.09.001},
  volume       = {1607},
  year         = {2003},
}