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Volumn 52, Issue 50, 2013, Pages 8993-9000

Characterization of two quinone radicals in the NADH:Ubiquinone oxidoreductase from Escherichia coli by a combined fluorescence spectroscopic and electrochemical approach

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROCHEMICAL REDOX; ELECTRON-TRANSFER CHAIN; FLAVIN MONONUCLEOTIDES; FLUORESCENCE EMISSION; FLUORESCENCE EXCITATION; MIDPOINT POTENTIALS; NADH DEHYDROGENASE; STANDARD HYDROGEN ELECTRODES;

EID: 84890493866     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4009903     Document Type: Article
Times cited : (13)

References (54)
  • 1
    • 0025760073 scopus 로고
    • The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss, H., Friedrich, T., Hofhaus, G., and Preis, D. (1991) The respiratory-chain NADH dehydrogenase (complex I) of mitochondria Eur. J. Biochem. 197, 563-576
    • (1991) Eur. J. Biochem. , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4
  • 2
    • 0025991887 scopus 로고
    • Redox-linked proton translocation by NADH-ubiquinone reductase (complex I)
    • Weiss, H. and Friedrich, T. (1991) Redox-linked proton translocation by NADH-ubiquinone reductase (complex I) J. Bioenerg. Biomembr. 23, 743-754
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 743-754
    • Weiss, H.1    Friedrich, T.2
  • 3
    • 0027104114 scopus 로고
    • The NADH: Ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker, J. E. (1992) The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains Q. Rev. Biophys. 25, 253-324 (Pubitemid 23014370)
    • (1992) Quarterly Reviews of Biophysics , vol.25 , Issue.3 , pp. 253-324
    • Walker, J.E.1
  • 5
  • 6
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex i of bacteria and mitochondria and its homologue in chloroplasts
    • Friedrich, T., Steinmuller, K., and Weiss, H. (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts FEBS Lett. 367, 107-111
    • (1995) FEBS Lett. , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmuller, K.2    Weiss, H.3
  • 8
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • DOI 10.1016/S0014-5793(00)01867-6, PII S0014579300018676
    • Friedrich, T. and Scheide, D. (2000) The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases FEBS Lett. 479, 1-5 (Pubitemid 30625247)
    • (2000) FEBS Letters , vol.479 , Issue.1-2 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 9
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (Complex I) at 22 Å in ice
    • DOI 10.1006/jmbi.1998.1668
    • Grigorieff, N. (1998) Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice J. Mol. Biol. 277, 1033-1046 (Pubitemid 28190844)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.5 , pp. 1033-1046
    • Grigorieff, N.1
  • 10
    • 0037124043 scopus 로고    scopus 로고
    • A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
    • DOI 10.1074/jbc.M112357200
    • Bottcher, B., Scheide, D., Hesterberg, M., Nagel-Steger, L., and Friedrich, T. (2002) A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) J. Biol. Chem. 277, 17970-17977 (Pubitemid 34967608)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 17970-17977
    • Bottcher, B.1    Scheide, D.2    Hesterberg, M.3    Nagel-Steger, L.4    Friedrich, T.5
  • 11
    • 33846270288 scopus 로고    scopus 로고
    • Projection Structure of the Membrane Domain of Escherichia coli Respiratory Complex I at 8 Å Resolution
    • DOI 10.1016/j.jmb.2006.11.026, PII S0022283606015634
    • Baranova, E. A., Holt, P. J., and Sazanov, L. A. (2007) Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 Å resolution J. Mol. Biol. 366, 140-154 (Pubitemid 46123333)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 140-154
    • Baranova, E.A.1    Holt, P.J.2    Sazanov, L.A.3
  • 12
    • 0037418550 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: The secret unlocked
    • DOI 10.1021/bi027158b
    • Yagi, T. and Matsuno-Yagi, A. (2003) The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: The secret unlocked Biochemistry 42, 2266-2274 (Pubitemid 36255200)
    • (2003) Biochemistry , vol.42 , Issue.8 , pp. 2266-2274
    • Yagi, T.1    Matsuno-Yagi, A.2
  • 13
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • DOI 10.1126/science.1123809
    • Sazanov, L. A. and Hinchliffe, P. (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus Science 311, 1430-1436 (Pubitemid 43376691)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 14
    • 0038392255 scopus 로고    scopus 로고
    • Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism?
    • DOI 10.1016/S0014-5793(03)00387-9
    • Brandt, U., Kerscher, S., Drose, S., Zwicker, K., and Zickermann, V. (2003) Proton pumping by NADH:ubiquinone oxidoreductase. A redox driven conformational change mechanism? FEBS Lett. 545, 9-17 (Pubitemid 36629630)
    • (2003) FEBS Letters , vol.545 , Issue.1 , pp. 9-17
    • Brandt, U.1    Kerscher, S.2    Drose, S.3    Zwicker, K.4    Zickermann, V.5
  • 15
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • DOI 10.1021/bi602508x
    • Sazanov, L. A. (2007) Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain Biochemistry 46, 2275-2288 (Pubitemid 46362402)
    • (2007) Biochemistry , vol.46 , Issue.9 , pp. 2275-2288
    • Sazanov, L.A.1
  • 16
    • 24044481623 scopus 로고    scopus 로고
    • Conformation-driven and semiquinone-gated proton-pump mechanism in the NADH-ubiquinone oxidoreductase (complex I)
    • DOI 10.1016/j.febslet.2005.06.086, PII S0014579305008641
    • Ohnishi, T. and Salerno, J. C. (2005) Conformation-driven and semiquinone-gated proton-pump mechanism in the NADH-ubiquinone oxidoreductase (complex I) FEBS Lett. 579, 4555-4561 (Pubitemid 41218626)
    • (2005) FEBS Letters , vol.579 , Issue.21 , pp. 4555-4561
    • Ohnishi, T.1    Salerno, J.C.2
  • 17
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex i
    • Efremov, R. G., Baradaran, R., and Sazanov, L. A. (2010) The architecture of respiratory complex I Nature 465, 441-445
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 18
    • 84864659415 scopus 로고    scopus 로고
    • The coupling mechanism of respiratory complex I: A structural and evolutionary perspective
    • Efremov, R. G. and Sazanov, L. A. (2012) The coupling mechanism of respiratory complex I: A structural and evolutionary perspective Biochim. Biophys. Acta 1817, 1785-1795
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1785-1795
    • Efremov, R.G.1    Sazanov, L.A.2
  • 19
    • 84874352529 scopus 로고    scopus 로고
    • Crystal structure of the entire respiratory complex i
    • Baradaran, R., Berrisford, J. M., Minhas, G. S., and Sazanov, L. A. (2013) Crystal structure of the entire respiratory complex I Nature 494, 443-448
    • (2013) Nature , vol.494 , pp. 443-448
    • Baradaran, R.1    Berrisford, J.M.2    Minhas, G.S.3    Sazanov, L.A.4
  • 20
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex i
    • Hunte, C., Zickermann, V., and Brandt, U. (2010) Functional modules and structural basis of conformational coupling in mitochondrial complex I Science 329, 448-451
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 22
    • 34249895284 scopus 로고    scopus 로고
    • Iron-sulfur cluster N7 of the NADH:Ubiquinone oxidoreductase (complex I) is essential for stability but not involved in electron transfer
    • DOI 10.1021/bi700371c
    • Pohl, T., Bauer, T., Dorner, K., Stolpe, S., Sell, P., Zocher, G., and Friedrich, T. (2007) Iron-sulfur cluster N7 of the NADH:ubiquinone oxidoreductase (complex I) is essential for stability but not involved in electron transfer Biochemistry 46, 6588-6596 (Pubitemid 46870124)
    • (2007) Biochemistry , vol.46 , Issue.22 , pp. 6588-6596
    • Pohl, T.1    Bauer, T.2    Dorner, K.3    Stolpe, S.4    Sell, P.5    Zocher, G.6    Friedrich, T.7
  • 23
    • 52949114593 scopus 로고    scopus 로고
    • Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of complex i from Escherichia coli and Thermus thermophilus
    • Berrisford, J. M., Thompson, C. J., and Sazanov, L. A. (2008) Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of complex I from Escherichia coli and Thermus thermophilus Biochemistry 47, 10262-10270
    • (2008) Biochemistry , vol.47 , pp. 10262-10270
    • Berrisford, J.M.1    Thompson, C.J.2    Sazanov, L.A.3
  • 24
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in Complex I
    • DOI 10.1016/S0005-2728(98)00027-9, PII S0005272898000279
    • Ohnishi, T. (1998) Iron-sulfur clusters/semiquinones in complex I Biochim. Biophys. Acta 1364, 186-206 (Pubitemid 28291839)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1364 , Issue.2 , pp. 186-206
    • Ohnishi, T.1
  • 25
    • 78149467471 scopus 로고    scopus 로고
    • Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I)
    • Ohnishi, S. T., Salerno, J. C., and Ohnishi, T. (2010) Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I) Biochim. Biophys. Acta 1797, 1891-1893
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1891-1893
    • Ohnishi, S.T.1    Salerno, J.C.2    Ohnishi, T.3
  • 26
    • 84877902640 scopus 로고    scopus 로고
    • Semiquinone and Cluster N6 Signals in His-tagged Proton-translocating NADH:Ubiquinone Oxidoreductase (Complex I) from Escherichia coli
    • Narayanan, M., Gabrieli, D. J., Leung, S. A., Elguindy, M. M., Glaser, C. A., Saju, N., Sinha, S. C., and Nakamaru-Ogiso, E. (2013) Semiquinone and Cluster N6 Signals in His-tagged Proton-translocating NADH:Ubiquinone Oxidoreductase (Complex I) from Escherichia coli J. Biol. Chem. 288, 14310-14319
    • (2013) J. Biol. Chem. , vol.288 , pp. 14310-14319
    • Narayanan, M.1    Gabrieli, D.J.2    Leung, S.A.3    Elguindy, M.M.4    Glaser, C.A.5    Saju, N.6    Sinha, S.C.7    Nakamaru-Ogiso, E.8
  • 28
    • 0032434231 scopus 로고    scopus 로고
    • Search for novel redox groups in mitochondrial NADH:Ubiquinone oxidoreductase (complex I) by diode array UV/VIS spectroscopy
    • Schulte, U., Abelmann, A., Amling, N., Brors, B., Friedrich, T., Kintscher, L., Rasmussen, T., and Weiss, H. (1998) Search for novel redox groups in mitochondrial NADH:ubiquinone oxidoreductase (complex I) by diode array UV/VIS spectroscopy Biofactors 8, 177-186 (Pubitemid 29021345)
    • (1998) BioFactors , vol.8 , Issue.3-4 , pp. 177-186
    • Schulte, U.1    Abelmann, A.2    Amling, N.3    Brors, B.4    Friedrich, T.5    Kintscher, L.6    Rasmussen, T.7    Weiss, H.8
  • 29
    • 34548683897 scopus 로고    scopus 로고
    • Lambda red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:Ubiquinone oxidoreductase (complex I)
    • DOI 10.1021/bi701057t
    • Pohl, T., Uhlmann, M., Kaufenstein, M., and Friedrich, T. (2007) Lambda Red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) Biochemistry 46, 10694-10702 (Pubitemid 47417261)
    • (2007) Biochemistry , vol.46 , Issue.37 , pp. 10694-10702
    • Pohl, T.1    Uhlmann, M.2    Kaufenstein, M.3    Friedrich, T.4
  • 30
    • 0032539640 scopus 로고    scopus 로고
    • Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • DOI 10.1021/bi971176p
    • Braun, M., Bungert, S., and Friedrich, T. (1998) Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli Biochemistry 37, 1861-1867 (Pubitemid 28099808)
    • (1998) Biochemistry , vol.37 , Issue.7 , pp. 1861-1867
    • Braun, M.1    Bungert, S.2    Friedrich, T.3
  • 31
    • 0032726773 scopus 로고    scopus 로고
    • One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography
    • DOI 10.1016/S0014-5793(99)01341-1, PII S0014579399013411
    • Bungert, S., Krafft, B., Schlesinger, R., and Friedrich, T. (1999) One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography FEBS Lett. 460, 207-211 (Pubitemid 29495941)
    • (1999) FEBS Letters , vol.460 , Issue.2 , pp. 207-211
    • Bungert, S.1    Krafft, B.2    Schlesinger, R.3    Friedrich, T.4
  • 32
    • 78650919425 scopus 로고    scopus 로고
    • A combined fluorescence spectroscopic and electrochemical approach for the study of thioredoxins
    • Voicescu, M., Rother, D., Bardischewsky, F., Friedrich, C. G., and Hellwig, P. (2011) A combined fluorescence spectroscopic and electrochemical approach for the study of thioredoxins Biochemistry 50, 17-24
    • (2011) Biochemistry , vol.50 , pp. 17-24
    • Voicescu, M.1    Rother, D.2    Bardischewsky, F.3    Friedrich, C.G.4    Hellwig, P.5
  • 33
    • 0025115245 scopus 로고
    • Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c
    • Moss, D., Nabedryk, E., Breton, J., and Mantele, W. (1990) Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c Eur. J. Biochem. 187, 565-572 (Pubitemid 20074919)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.3 , pp. 565-572
    • Moss, D.1    Nabedryk, E.2    Breton, J.3    Mantele, W.4
  • 34
    • 0032546595 scopus 로고    scopus 로고
    • Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy
    • DOI 10.1021/bi9725576
    • Hellwig, P., Behr, J., Ostermeier, C., Richter, O. M., Pfitzner, U., Odenwald, A., Ludwig, B., Michel, H., and Mantele, W. (1998) Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy Biochemistry 37, 7390-7399 (Pubitemid 28235222)
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7390-7399
    • Hellwig, P.1    Behr, J.2    Ostermeier, C.3    Richter, O.-M.H.4    Pfitzner, U.5    Odenwald, A.6    Ludwig, B.7    Michel, H.8    Mantele, W.9
  • 35
    • 0034609560 scopus 로고    scopus 로고
    • FT-IR spectroscopic characterization of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain
    • Hellwig, P., Scheide, D., Bungert, S., Mantele, W., and Friedrich, T. (2000) FT-IR spectroscopic characterization of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain Biochemistry 39, 10884-10891
    • (2000) Biochemistry , vol.39 , pp. 10884-10891
    • Hellwig, P.1    Scheide, D.2    Bungert, S.3    Mantele, W.4    Friedrich, T.5
  • 36
    • 0001059223 scopus 로고
    • Electrochemical and infrared-spectroscopic characterization of redox reactions of p-quinones
    • Bauscher, M. and Maentele, W. (1992) Electrochemical and infrared-spectroscopic characterization of redox reactions of p-quinones J. Phys. Chem. 96, 11101-11108
    • (1992) J. Phys. Chem. , vol.96 , pp. 11101-11108
    • Bauscher, M.1    Maentele, W.2
  • 37
    • 2442473296 scopus 로고    scopus 로고
    • The Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I) Is a Primary Proton Pump but May Be Capable of Secondary Sodium Antiport
    • DOI 10.1074/jbc.M311242200
    • Stolpe, S. and Friedrich, T. (2004) The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport J. Biol. Chem. 279, 18377-18383 (Pubitemid 38623253)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18377-18383
    • Stolpe, S.1    Friedrich, T.2
  • 38
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer, L. (1978) Fluorescence energy transfer as a spectroscopic ruler Annu. Rev. Biochem. 47, 819-846
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 40
    • 14044276977 scopus 로고    scopus 로고
    • Distribution of mitochondrial NADH fluorescence lifetimes: Steady-state kinetics of matrix NADH interactions
    • DOI 10.1021/bi0485124
    • Blinova, K., Carroll, S., Bose, S., Smirnov, A. V., Harvey, J. J., Knutson, J. R., and Balaban, R. S. (2005) Distribution of mitochondrial NADH fluorescence lifetimes: Steady-state kinetics of matrix NADH interactions Biochemistry 44, 2585-2594 (Pubitemid 40279562)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2585-2594
    • Blinova, K.1    Carroll, S.2    Bose, S.3    Smirnov, A.V.4    Harvey, J.J.5    Knutson, J.R.6    Balaban, R.S.7
  • 41
    • 0024454693 scopus 로고
    • Photoreduction fluorescence detection of quinones in high-performance liquid chromatography
    • Poulsen, J. R. and Birks, J. W. (1989) Photoreduction Fluorescence Detection of quinones in High-Performance Liquid Chromatography Anal. Chem. 61, 2267-2276 (Pubitemid 19252821)
    • (1989) Analytical Chemistry , vol.61 , Issue.20 , pp. 2267-2276
    • Poulsen, J.R.1    Birks, J.W.2
  • 42
    • 0031254695 scopus 로고    scopus 로고
    • In-situ photochemical spectrofluorimetric detection of 9,10-anthraquinone-labeled bovine serum albumin
    • Zhu, Q. Z., Xu, J. G., Guo, X. Q., Zheng, X. Y., Li, W. Y., and Zhao, Y. B. (1997) In-situ photochemical spectrofluorimetric detection of 9,10-anthraquinone-labeled bovine serum albumin Spectrochim. Acta, Part A 53A, 2195-2200
    • (1997) Spectrochim. Acta, Part A , vol.53 , pp. 2195-2200
    • Zhu, Q.Z.1    Xu, J.G.2    Guo, X.Q.3    Zheng, X.Y.4    Li, W.Y.5    Zhao, Y.B.6
  • 43
    • 27644534271 scopus 로고    scopus 로고
    • Fluorescence spectroscopy reveals ubiquitous presence of oxidized and reduced quinones in dissolved organic matter
    • DOI 10.1021/es0506962
    • Cory, R. M. and McKnight, D. M. (2005) Fluorescence spectroscopy reveals ubiquitous presence of oxidized and reduced quinones in dissolved organic matter Environ. Sci. Technol. 39, 8142-8149 (Pubitemid 41572395)
    • (2005) Environmental Science and Technology , vol.39 , Issue.21 , pp. 8142-8149
    • Cory, R.M.1    McKnight, D.M.2
  • 44
    • 0006894480 scopus 로고    scopus 로고
    • UV-visible spectroelectrochemistry of reduction products of anthraquinone in dimethylformamide solutions
    • Babaei, A., Connor, P. A., McQuillan, A. J., and Umapathy, S. (1997) UV-visible spectroelectrochemistry of reduction products of anthraquinone in dimethylformamide solutions J. Chem. Educ. 74, 1200-1204
    • (1997) J. Chem. Educ. , vol.74 , pp. 1200-1204
    • Babaei, A.1    Connor, P.A.2    McQuillan, A.J.3    Umapathy, S.4
  • 45
    • 0027990677 scopus 로고
    • Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Sled, V. D., Rudnitzky, N. I., Hatefi, Y., and Ohnishi, T. (1994) Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I) Biochemistry 33, 10069-10075 (Pubitemid 24286086)
    • (1994) Biochemistry , vol.33 , Issue.33 , pp. 10069-10075
    • Sled, V.D.1    Rudnitzky, N.I.2    Hatefi, Y.3    Ohnishi, T.4
  • 47
    • 0037096980 scopus 로고    scopus 로고
    • Disruption of iron-sulphur cluster N2 from NADH:ubiquinone oxidoreductase by site-directed mutagenesis
    • DOI 10.1042/BJ20011750
    • Duarte, M., Populo, H., Videira, A., Friedrich, T., and Schulte, U. (2002) Disruption of iron-sulphur cluster N2 from NADH:ubiquinone oxidoreductase by site-directed mutagenesis Biochem. J. 364, 833-839 (Pubitemid 34680860)
    • (2002) Biochemical Journal , vol.364 , Issue.3 , pp. 833-839
    • Duarte, M.1    Populo, H.2    Videira, A.3    Friedrich, T.4    Schulte, U.5
  • 49
    • 0033547703 scopus 로고    scopus 로고
    • B in Photosystem II Is Thermodynamically Perturbed in Phototolerant Mutants of Synechocystis sp. PCC 6803
    • B in Photosystem II Is Thermodynamically Perturbed in Phototolerant Mutants of Synechocystis sp. PCC 6803 Biochemistry 38, 770-775
    • (1999) Biochemistry , vol.38 , pp. 770-775
    • Minagawa, J.1    Narusaka, Y.2    Inoue, Y.3    Satoh, K.4
  • 50
    • 78249233837 scopus 로고    scopus 로고
    • Probing the quinone binding site of Photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides
    • Boussac, A., Sugiura, M., and Rappaport, F. (2011) Probing the quinone binding site of Photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides Biochim. Biophys. Acta 1807, 119-129
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 119-129
    • Boussac, A.1    Sugiura, M.2    Rappaport, F.3
  • 51
    • 0035797872 scopus 로고    scopus 로고
    • Kinetics of Electron Transfer from QA to QB in Photosystem II
    • de Wijn, R. and van Gorkom, H. J. (2001) Kinetics of Electron Transfer from QA to QB in Photosystem II Biochemistry 40, 11912-11922
    • (2001) Biochemistry , vol.40 , pp. 11912-11922
    • De Wijn, R.1    Van Gorkom, H.J.2
  • 52
    • 33845750131 scopus 로고    scopus 로고
    • Investigation of the mechanism of proton translocation by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria: Does the enzyme operate by a Q-cycle mechanism?
    • DOI 10.1042/BJ20060766
    • Sherwood, S. and Hirst, J. (2006) Investigation of the mechanism of proton translocation by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria: Does the enzyme operate by a Q-cycle mechanism? Biochem. J. 400, 541-550 (Pubitemid 44974466)
    • (2006) Biochemical Journal , vol.400 , Issue.3 , pp. 541-550
    • Sherwood, S.1    Hirst, J.2
  • 53
    • 3342951743 scopus 로고    scopus 로고
    • Determination of enzyme mechanisms by molecular dynamics: Studies on quinoproteins, methanol dehydrogenase, and soluble glucose dehydrogenase
    • DOI 10.1110/ps.04673404
    • Reddy, S. Y. and Bruice, T. C. (2004) Determination of enzyme mechanisms by molecular dynamics: Studies on quinoproteins, methanol dehydrogenase, and soluble glucose dehydrogenase Protein Sci. 13, 1965-1978 (Pubitemid 38989604)
    • (2004) Protein Science , vol.13 , Issue.8 , pp. 1965-1978
    • Reddy, S.Y.1    Bruice, T.C.2
  • 54
    • 70349787152 scopus 로고    scopus 로고
    • Measurement of the molecular masses of hydrophilic and hydrophobic subunits of ATP synthase and complex i in a single experiment
    • Carroll, J., Fearnley, I. M., Wang, Q., and Walker, J. E. (2009) Measurement of the molecular masses of hydrophilic and hydrophobic subunits of ATP synthase and complex I in a single experiment Anal. Biochem. 395, 249-255
    • (2009) Anal. Biochem. , vol.395 , pp. 249-255
    • Carroll, J.1    Fearnley, I.M.2    Wang, Q.3    Walker, J.E.4


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