IOCAS-IR
Identification and characterization two isoforms of NADH:ubiquinone oxidoreductase from the hyperthermophilic eubacterium Aquifex aeolicus
Peng, Guohong1,5; Meyer, Bjorn2; Sokolova, Lucie3; Liu, Wenxia1; Bornemann, Sandra2; Juli, Jana1; Zwicker, Klaus4; Karas, Michael2; Brutschy, Bernd3; Michel, Hartmut1
2018-05-01
Source PublicationBIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
ISSN0005-2728
Volume1859Issue:5Pages:366-373
Corresponding AuthorPeng, Guohong(Guohong.Peng@biophys.mpg.de) ; Michel, Hartmut(Hartmut.Michel@biophys.mpg.de)
AbstractThe 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 NuoA(2), NuoB, NuoD(2), NuoE, NuoF, NuoG, Nuol(1), NuoH(1), NuoJ(1), NuoL(1), NuoM(1) and NuoN(1), with an entire mass of 504.17 kDa. NQOR2 comprises subunits NuoA(1), NuoB, NuoD(1), NuoE, NuoF, NuoG, NuoH(2), NuoI(2), NuoJ(1), NuoK(1), NuoL(2), NuoM(2) and NuoN(2), 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.
KeywordAquifex aeolicus Complex I Isoform enzyme NADH:ubiquinone oxidoreductase Bacteria
DOI10.1016/j.bbabio.2018.02.008
Indexed BySCI
Language英语
Funding ProjectDeutsche Forschungsgemeinschaft[SFB 628] ; Deutsche Forschungsgemeinschaft (Cluster of Excellence Macromolecular Complexes Frankfurt) ; Max-Planck-Gesellschaft
WOS Research AreaBiochemistry & Molecular Biology ; Biophysics
WOS SubjectBiochemistry & Molecular Biology ; Biophysics
WOS IDWOS:000430881200007
PublisherELSEVIER SCIENCE BV
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/158924
Collection中国科学院海洋研究所
Corresponding AuthorPeng, Guohong; Michel, Hartmut
Affiliation1.Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany
2.Goethe Univ, Inst Pharmaceut Chem, D-60438 Frankfurt, Germany
3.Goethe Univ, Inst Phys & Theoret Chem, D-60438 Frankfurt, Germany
4.Goethe Univ Frankfurt, Inst Biochem 1, Fac Med, D-60590 Frankfurt, Germany
5.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China
First Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Corresponding Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Recommended Citation
GB/T 7714
Peng, Guohong,Meyer, Bjorn,Sokolova, Lucie,et al. Identification and characterization two isoforms of NADH:ubiquinone oxidoreductase from the hyperthermophilic eubacterium Aquifex aeolicus[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,2018,1859(5):366-373.
APA Peng, Guohong.,Meyer, Bjorn.,Sokolova, Lucie.,Liu, Wenxia.,Bornemann, Sandra.,...&Michel, Hartmut.(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.
MLA Peng, Guohong,et al."Identification and characterization two isoforms of NADH:ubiquinone oxidoreductase from the hyperthermophilic eubacterium Aquifex aeolicus".BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1859.5(2018):366-373.
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