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Sodium influence on energy transduction by complexes I from Escherichia coli and Paracoccus denitrificans
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The nature of the ions that are translocated by Escherichia coli and Paracoccus denitrificans complexes I was investigated. We observed that E. coli complex I was capable of proton translocation in the same direction to the established deltapsi, showing that in the tested conditions, the coupling ion is the H(+). Furthermore, Na(+) transport to the opposite direction was also observed, and, although Na(+) was not necessary for the catalytic or proton transport activities, its presence increased the latter. We also observed H(+) translocation by P. denitrificans complex I, but in this case, H(+) transport was not influenced by Na(+) and also Na(+) transport was not observed. We concluded that E. coli complex I has two energy coupling sites (one Na(+) independent and the other Na(+) dependent), as previously observed for Rhodothermus marinus complex I, whereas the coupling mechanism of P. denitrificans enzyme is completely Na(+) independent. This work thus shows that complex I energy transduction by proton pumping and Na(+)/H(+) antiporting is not exclusive of the R. marinus enzyme. Nevertheless, the Na(+)/H(+) antiport activity seems not to be a general property of complex I, which may be correlated with the metabolic characteristics of the organisms.
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“complex I itself possesses some of the same Na+/H+ promiscuity [206] as Ech and the ATP synthase do.”
From Early bioenergetic evolution (2013) · cites this paper as [206]
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Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
Sazanov, L. A., & Hinchliffe, P. (2006) · Science · doi:10.1126/science.1123809 · Cited by 763
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Sousa, F. L., Thiergart, T., Landan, G., Nelson-Sathi, S., Pereira, I. A. C., Allen, J. F., Lane, N., & Martin, W. F. (2013) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0088 · Cited by 286
“In this case, it is also noteworthy that complex I itself possesses some of the same Naþ/Hþ promiscuity [206] as Ech and the ATP synthase do.”
BackgroundA missing link between complex I and group 4 membrane-bound [NiFe] hydrogenases
Marreiros, B. C., Batista, A. P., Duarte, A. M. S., & Pereira, M. M. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.09.012 · Cited by 120
Self-citation
Metadata
- Authors
- Batista, A. P., & Pereira, M. M.
- Affiliations
- Universidade Nova de Lisboa (PT)
- Corresponding author
- Pereira, Manuela M.
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2011-03
- Volume
- 1807
- Issue
- 3
- Pages
- 286-292
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2038634941
- Cited by
- 20
- References
- 1
- Citations by year
- 2024: 1 · 2021: 2 · 2019: 1 · 2018: 1 · 2017: 1 · 2015: 2 · 2014: 2 · 2013: 4 · 2012: 6
- FWCI
- 1.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Biochimica et Biophysica Acta
- Funders
- FCT, Projecto de Re-Equipamento Científico (REDE/1517/RMN/2005)
- Fundação para a Ciência e a Tecnologia (SFRH/BD/25288/2005, POCI/QUI-BIQ/100302/2008)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- complex I, NADH dehydrogenase, sodium ions, proton translocation, Na+/H+ antiport, energy transduction, Escherichia coli, Paracoccus denitrificans, Rhodothermus marinus, ion translocation
- MeSH terms
- Biological Transport, Cell Membrane, Energy Metabolism, Escherichia coli, Hydrogen-Ion Concentration, Kinetics, Membrane Potentials, NAD, Magnetic Resonance Spectroscopy, Oxidoreductases, Oxygen Consumption, Paracoccus denitrificans, Protons, Sodium, Ion Transport, Electron Transport Complex I, Rhodothermus
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