메뉴 건너뛰기




Volumn 456, Issue A, 2009, Pages 75-93

Chapter 4 Electron Transfer in Respiratory Complexes Resolved by an Ultra-Fast Freeze-Quench Approach

Author keywords

[No Author keywords available]

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 63449085768     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)04404-2     Document Type: Review
Times cited : (8)

References (19)
  • 1
    • 0018110976 scopus 로고
    • Freeze-quench and chemical-quench techniques
    • Ballou D.P. Freeze-quench and chemical-quench techniques. Methods Enzymol. 54 (1978) 85-93
    • (1978) Methods Enzymol. , vol.54 , pp. 85-93
    • Ballou, D.P.1
  • 2
    • 33846240878 scopus 로고    scopus 로고
    • Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli
    • Belevich G., Euro L., Wikström M., and Verkhovskaya M. Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli. Biochemistry 46 (2007) 526-533
    • (2007) Biochemistry , vol.46 , pp. 526-533
    • Belevich, G.1    Euro, L.2    Wikström, M.3    Verkhovskaya, M.4
  • 3
    • 0018024483 scopus 로고
    • Some problems concerning mixers and detectors for stopped flow kinetic studies
    • Berger R.L. Some problems concerning mixers and detectors for stopped flow kinetic studies. Biophys. J. 24 (1978) 2-20
    • (1978) Biophys. J. , vol.24 , pp. 2-20
    • Berger, R.L.1
  • 4
    • 29744445466 scopus 로고    scopus 로고
    • A microchannel solution mixer for studying microsecond protein folding reactions
    • Bilsel O., Kayatekin C., Wallace L.A., and Matthews C.R. A microchannel solution mixer for studying microsecond protein folding reactions. Rev. Sci. Instrum. 76 (2005) 014302 1-7
    • (2005) Rev. Sci. Instrum. , vol.76
    • Bilsel, O.1    Kayatekin, C.2    Wallace, L.A.3    Matthews, C.R.4
  • 5
    • 2342618805 scopus 로고    scopus 로고
    • Microsecond freeze-hyperquenching: Development of a new ultrafast micro-mixing and sampling technology and application to enzyme catalysis
    • Cherepanov A.V., and de Vries S. Microsecond freeze-hyperquenching: Development of a new ultrafast micro-mixing and sampling technology and application to enzyme catalysis. Biochim. Biophys. Acta 1656 (2004) 1-31
    • (2004) Biochim. Biophys. Acta , vol.1656 , pp. 1-31
    • Cherepanov, A.V.1    de Vries, S.2
  • 6
    • 0032588194 scopus 로고    scopus 로고
    • - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • - stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. FEBS Lett. 451 (1999) 157-161
    • (1999) FEBS Lett. , vol.451 , pp. 157-161
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 7
    • 2442701768 scopus 로고    scopus 로고
    • Functional significance of conserved histidines and arginines in the 49-kDa subunit of mitochondrial complex I
    • Grgic L., Zwicker K., Kashani-Poor N., Kerscher S., and Brandt U. Functional significance of conserved histidines and arginines in the 49-kDa subunit of mitochondrial complex I. J. Biol. Chem. 279 (2004) 21193-21199
    • (2004) J. Biol. Chem. , vol.279 , pp. 21193-21199
    • Grgic, L.1    Zwicker, K.2    Kashani-Poor, N.3    Kerscher, S.4    Brandt, U.5
  • 8
    • 0028916224 scopus 로고
    • Rapid quench kinetic analysis of polymerases, adenosinetriphosphatases, and enzyme intermediates
    • Johnson K.A. Rapid quench kinetic analysis of polymerases, adenosinetriphosphatases, and enzyme intermediates. Methods Enzymol. 249 (1995) 38-61
    • (1995) Methods Enzymol. , vol.249 , pp. 38-61
    • Johnson, K.A.1
  • 9
    • 0142072511 scopus 로고    scopus 로고
    • Ultrafast microfluidic mixer and freeze-quenching device
    • Lin Y., Gerfen G.J., Rousseau D.L., and Yeh S.R. Ultrafast microfluidic mixer and freeze-quenching device. Anal. Chem. 75 (2003) 5381-5386
    • (2003) Anal. Chem. , vol.75 , pp. 5381-5386
    • Lin, Y.1    Gerfen, G.J.2    Rousseau, D.L.3    Yeh, S.R.4
  • 10
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in complex I
    • Ohnishi T. Iron-sulfur clusters/semiquinones in complex I. Biochim. Biophys. Acta 1364 (1998) 186-206
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 12
    • 3242883536 scopus 로고    scopus 로고
    • Rapid mixing methods for exploring the kinetics of protein folding
    • Roder H., Maki K., Cheng H., and Shastry M.C. Rapid mixing methods for exploring the kinetics of protein folding. Methods 34 (2004) 15-27
    • (2004) Methods , vol.34 , pp. 15-27
    • Roder, H.1    Maki, K.2    Cheng, H.3    Shastry, M.C.4
  • 14
    • 0031969090 scopus 로고    scopus 로고
    • A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale
    • Shastry M.C., Luck S.D., and Roder H. A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale. Biophys. J. 74 (1998) 2714-2721
    • (1998) Biophys. J. , vol.74 , pp. 2714-2721
    • Shastry, M.C.1    Luck, S.D.2    Roder, H.3
  • 15
    • 20444430872 scopus 로고    scopus 로고
    • Activation of isolated NADH:ubiquinone reductase I (complex I) from Escherichia coli by detergent and phospholipids. Recovery of ubiquinone reductase activity and changes in EPR signals of iron-sulfur clusters
    • Sinegina L., Wikström M., Verkhovsky M.I., and Verkhovskaya M.L. Activation of isolated NADH:ubiquinone reductase I (complex I) from Escherichia coli by detergent and phospholipids. Recovery of ubiquinone reductase activity and changes in EPR signals of iron-sulfur clusters. Biochemistry 44 (2005) 8500-8506
    • (2005) Biochemistry , vol.44 , pp. 8500-8506
    • Sinegina, L.1    Wikström, M.2    Verkhovsky, M.I.3    Verkhovskaya, M.L.4
  • 16
    • 0015838168 scopus 로고
    • Observations relating to the efficiency of mixing in rapid reaction flow devices
    • Smith M.H. Observations relating to the efficiency of mixing in rapid reaction flow devices. Biophys. J. 13 (1973) 817-821
    • (1973) Biophys. J. , vol.13 , pp. 817-821
    • Smith, M.H.1
  • 17
    • 0037339302 scopus 로고    scopus 로고
    • Activation of hydrogen peroxide in horseradish peroxidase occurs within approximately 200 micros observed by a new freeze-quench device
    • Tanaka M., Matsuura K., Yoshioka S., Takahashi S., Ishimori K., Hori H., and Morishima I. Activation of hydrogen peroxide in horseradish peroxidase occurs within approximately 200 micros observed by a new freeze-quench device. Biophys. J. 84 (2003) 1998-2004
    • (2003) Biophys. J. , vol.84 , pp. 1998-2004
    • Tanaka, M.1    Matsuura, K.2    Yoshioka, S.3    Takahashi, S.4    Ishimori, K.5    Hori, H.6    Morishima, I.7
  • 19
    • 0021769852 scopus 로고
    • Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone
    • Wikström M. Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone. FEBS Lett. 169 (1984) 300-304
    • (1984) FEBS Lett. , vol.169 , pp. 300-304
    • Wikström, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.