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  Identification and characterization two isoforms of NADH:ubiquinone oxidoreductase from the hyperthermophilic eubacterium Aquifex aeolicus

Peng, G., Meyer, B., Sokolova, L., Liu, W., Bornemann, S., Juli, J., et al. (2018). Identification and characterization two isoforms of NADH:ubiquinone oxidoreductase from the hyperthermophilic eubacterium Aquifex aeolicus. Biochimica et Biophysica Acta, Bioenergetics, 1859(5), 366-373. doi:10.1016/j.bbabio.2018.02.008.

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 Creators:
Peng, Guohong1, 2, Author              
Meyer, Björn3, Author
Sokolova, Lucie4, Author
Liu, Wenxia1, Author              
Bornemann, Sandra3, Author
Juli, Jana1, Author              
Zwicker, Klaus5, Author
Karas, Michael3, Author
Brutschy, Bernd4, Author
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China, ou_persistent22              
3Institute of Pharmaceutical Chemistry, Goethe University, D-60438 Frankfurt, Germany, ou_persistent22              
4Institute of Physics and Theoretical Chemistry, Goethe University, D-60438 Frankfurt, Germany, ou_persistent22              
5Institute of Biochemistry I, Faculty of Medicine, Goethe-University Frankfurt, D-60590 Frankfurt, Germany, ou_persistent22              

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Free keywords: Aquifex aeolicus; Complex I; Isoform enzyme; NADH:ubiquinone oxidoreductase; Bacteria
 Abstract: The NADH:ubiquinone oxidoreductase (complex I) is the first enzyme of the respiratory chain and the entry point for most electrons. Generally, the bacterial complex I consists of 14 core subunits, homologues of which are also found in complex I of mitochondria. In complex I preparations from the hyperthermophilic bacterium Aquifex aeolicus we have identified 20 partially homologous subunits by combining MALDI-TOF and LILBID mass spectrometry methods. The subunits could be assigned to two different complex I isoforms, named NQOR1 and NQOR2. NQOR1 consists of subunits NuoA2, NuoB, NuoD2, NuoE, NuoF, NuoG, NuoI1, NuoH1, NuoJ1, NuoK1, NuoL1, NuoM1 and NuoN1, with an entire mass of 504.17 kDa. NQOR2 comprises subunits NuoA1, NuoB, NuoD1, NuoE, NuoF, NuoG, NuoH2, NuoI2, NuoJ1, NuoK1, NuoL2, NuoM2 and NuoN2, with a total mass of 523.99 kDa. Three Fe-S clusters could be identified by EPR spectroscopy in a preparation containing predominantly NQOR1. These were tentatively assigned to a binuclear center N1, and two tetranuclear centers, N2 and N4. The redox midpoint potentials of N1 and N2 are −273 mV and −184 mV, respectively. Specific activity assays indicated that NQOR1 from cells grown under low concentrations of oxygen was the more active form. Increasing the concentration of oxygen in the bacterial cultures induced formation of NQOR2 showing the lower specific activity.

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Language(s): eng - English
 Dates: 2017-10-122018-02-242018-03-062018-05
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbabio.2018.02.008
 Degree: -

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Title: Biochimica et Biophysica Acta, Bioenergetics
  Abbreviation : Biochim. Biophys. Acta, Bioenerg.
Source Genre: Journal
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Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1859 (5) Sequence Number: - Start / End Page: 366 - 373 Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6