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Volumn 1787, Issue 10, 2009, Pages 1266-1271

Electrostatics of the FeS clusters in respiratory complex I

Author keywords

Complex I; Electron transfer; Iron sulfur cluster; NADH dehydrogenase; Poisson Boltzmann equation; Redox potential

Indexed keywords

IRON; SULFUR;

EID: 67649958261     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2009.05.001     Document Type: Article
Times cited : (19)

References (25)
  • 1
    • 21044445453 scopus 로고    scopus 로고
    • Energy transduction by respiratory complex I-an evaluation of current knowledge
    • Hirst J. Energy transduction by respiratory complex I-an evaluation of current knowledge. Biochem. Soc. T. 33 (2005) 525-529
    • (2005) Biochem. Soc. T. , vol.33 , pp. 525-529
    • Hirst, J.1
  • 2
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • Sazanov L. Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry 49 (2007) 2275-2288
    • (2007) Biochemistry , vol.49 , pp. 2275-2288
    • Sazanov, L.1
  • 4
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov L.A., and Hinchliffe P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311 (2006) 1430-1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 5
    • 46349107838 scopus 로고    scopus 로고
    • Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides
    • Morgan D.J., and Sazanov L.A. Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochim. Biophys. Acta 1777 (2008) 711-718
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 711-718
    • Morgan, D.J.1    Sazanov, L.A.2
  • 6
    • 34548361908 scopus 로고    scopus 로고
    • Direct localization of the 51 and 24 kDa subunits of mitochondrial complex I by three-dimensional difference imaging
    • Clason T., Zickermann V., Ruiz T., Brandt U., and Radermacher M. Direct localization of the 51 and 24 kDa subunits of mitochondrial complex I by three-dimensional difference imaging. J. Struct. Biol. 159 (2007) 433-442
    • (2007) J. Struct. Biol. , vol.159 , pp. 433-442
    • Clason, T.1    Zickermann, V.2    Ruiz, T.3    Brandt, U.4    Radermacher, M.5
  • 7
    • 24044481623 scopus 로고    scopus 로고
    • Conformation-driven and semiquinone-gated proton-pump mechanism in the NADH-ubiquinone oxidoreductase (complex I)
    • Ohnishi T., and Salerno J.C. Conformation-driven and semiquinone-gated proton-pump mechanism in the NADH-ubiquinone oxidoreductase (complex I). FEBS Lett. 579 (2005) 4555-4561
    • (2005) FEBS Lett. , vol.579 , pp. 4555-4561
    • Ohnishi, T.1    Salerno, J.C.2
  • 8
    • 34547917597 scopus 로고    scopus 로고
    • Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH:quinone oxidoreductase
    • Yakovlev G., Reda T., and Hirst J. Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH:quinone oxidoreductase. PNAS 104 (2007) 12720-12725
    • (2007) PNAS , vol.104 , pp. 12720-12725
    • Yakovlev, G.1    Reda, T.2    Hirst, J.3
  • 9
    • 50949130428 scopus 로고    scopus 로고
    • Were there any "misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?
    • Ohnishi T., and Nakamaru-Ogiso E. Were there any "misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?. Biochim. Biophys. Acta 1777 (2008) 703-710
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 703-710
    • Ohnishi, T.1    Nakamaru-Ogiso, E.2
  • 10
    • 40549126917 scopus 로고    scopus 로고
    • Electrostatic interactions between FeS clusters in NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • Euro L., Bloch D.A., Wikström M., Verkhovsky M.I., and Verkhovskaya M. Electrostatic interactions between FeS clusters in NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry 47 (2008) 3185-3193
    • (2008) Biochemistry , vol.47 , pp. 3185-3193
    • Euro, L.1    Bloch, D.A.2    Wikström, M.3    Verkhovsky, M.I.4    Verkhovskaya, M.5
  • 11
    • 84957665033 scopus 로고    scopus 로고
    • An object-oriented programming suite for electrostatic effects in biological molecules
    • Bashford D. An object-oriented programming suite for electrostatic effects in biological molecules. Scie. Comput. Object-Oriented Parallel Environ. 1343 (1997) 233-240
    • (1997) Scie. Comput. Object-Oriented Parallel Environ. , vol.1343 , pp. 233-240
    • Bashford, D.1
  • 12
    • 0026612756 scopus 로고
    • Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
    • Bashford D., and Gerwert K. Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin. J. Mol. Biol. 224 (1992) 473-486
    • (1992) J. Mol. Biol. , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 15
    • 49349116297 scopus 로고    scopus 로고
    • Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme
    • Sugitani R., Medvedev E.S., and Stuchebrukhov A.A. Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme. Biochim. Biophys. Acta 1777 (2008) 1129-1139
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1129-1139
    • Sugitani, R.1    Medvedev, E.S.2    Stuchebrukhov, A.A.3
  • 16
    • 0037440938 scopus 로고    scopus 로고
    • Calculation of the dielectric permittivity profile for a nonuniform system: application to a lipid bilayer simulation
    • Stern H., and Feller S. Calculation of the dielectric permittivity profile for a nonuniform system: application to a lipid bilayer simulation. J. Chem. Phys. 118 (2003) 3401-3412
    • (2003) J. Chem. Phys. , vol.118 , pp. 3401-3412
    • Stern, H.1    Feller, S.2
  • 17
    • 33744920795 scopus 로고    scopus 로고
    • Closer look at structure of fully hydrated fluid phase DPPC bilayers
    • Kucerka N., Tristram-Nagle S., and Nagle J. Closer look at structure of fully hydrated fluid phase DPPC bilayers. Biophys. J. 90 (2006) L83-L85
    • (2006) Biophys. J. , vol.90
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.3
  • 18
    • 0022964504 scopus 로고
    • Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: effects of ionic strength and amino-acid modification
    • Klapper I., Hagstrom R., Fine R., Sharp K., and Honig B. Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: effects of ionic strength and amino-acid modification. Proteins 1 (1986) 47-59
    • (1986) Proteins , vol.1 , pp. 47-59
    • Klapper, I.1    Hagstrom, R.2    Fine, R.3    Sharp, K.4    Honig, B.5
  • 19
    • 0001715782 scopus 로고    scopus 로고
    • Calculation of amino acid pK's in a protein from a continuum electrostatic model: method and sensitivity analysis
    • Beroza P., and Fredkin D.R. Calculation of amino acid pK's in a protein from a continuum electrostatic model: method and sensitivity analysis. J. Comp. Chem. 17 (1996) 1229-1244
    • (1996) J. Comp. Chem. , vol.17 , pp. 1229-1244
    • Beroza, P.1    Fredkin, D.R.2
  • 20
    • 0010624785 scopus 로고    scopus 로고
    • The effect of protein relaxation on charge-charge interactions and dielectric constants of proteins
    • Sham Y., Muegge I., and Warshel A. The effect of protein relaxation on charge-charge interactions and dielectric constants of proteins. Biophys. J. 74 (1998) 1744-1753
    • (1998) Biophys. J. , vol.74 , pp. 1744-1753
    • Sham, Y.1    Muegge, I.2    Warshel, A.3
  • 21
    • 54449087539 scopus 로고    scopus 로고
    • Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I)
    • Nakamaru-Ogiso E., Matsuno-Yagi A., Yoshikawa S., Yagi T., and Ohnishi T. Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I). J. Biol. Chem. 283 (2008) 25979-25987
    • (2008) J. Biol. Chem. , vol.283 , pp. 25979-25987
    • Nakamaru-Ogiso, E.1    Matsuno-Yagi, A.2    Yoshikawa, S.3    Yagi, T.4    Ohnishi, T.5
  • 22
    • 0014798606 scopus 로고
    • Effect of membrane potential on equilibrium poise between cytochrome a and cytochrome c in rat liver mitochondria
    • Hinkle P., and Mitchell P. Effect of membrane potential on equilibrium poise between cytochrome a and cytochrome c in rat liver mitochondria. Bioenergetics 1 (1970) 45-60
    • (1970) Bioenergetics , vol.1 , pp. 45-60
    • Hinkle, P.1    Mitchell, P.2
  • 23
    • 2542421934 scopus 로고    scopus 로고
    • Substrate-induced conformational change in bacterial complex I
    • Mamedova A.A., Holt P.J., Carroll J., and Sazanov L. Substrate-induced conformational change in bacterial complex I. J. Biol. Chem. 279 (2004) 23830-23836
    • (2004) J. Biol. Chem. , vol.279 , pp. 23830-23836
    • Mamedova, A.A.1    Holt, P.J.2    Carroll, J.3    Sazanov, L.4
  • 25
    • 1642451816 scopus 로고    scopus 로고
    • The gross structure of the respiratory complex I: a Lego system
    • Friedrich T., and Bottcher B. The gross structure of the respiratory complex I: a Lego system. Biochim. Biophys. Acta 1608 (2004) 1-9
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 1-9
    • Friedrich, T.1    Bottcher, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.