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Volumn 51, Issue 1, 2012, Pages 149-158

Mössbauer spectroscopy on respiratory complex I: The iron-sulfur cluster ensemble in the NADH-reduced enzyme is partially oxidized

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BOS TAURUS; CHAIN-EXTENDING; CLUSTER ENSEMBLES; COFACTORS; COUPLED SPINS; ELECTRON TRANSFER; EPR SIGNALS; EPR SPECTRA; EPR STUDIES; FLAVIN MONONUCLEOTIDES; INTRA-MOLECULAR ELECTRON TRANSFER; IRON-SULFUR CLUSTERS; OXIDOREDUCTASES; PROTON TRANSLOCATION; RESPIRATORY COMPLEX; SSBAUER SPECTROSCOPIES; STRUCTURAL DATA; YARROWIA LIPOLYTICA;

EID: 84856917379     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201644x     Document Type: Article
Times cited : (40)

References (70)
  • 1
    • 73849114263 scopus 로고    scopus 로고
    • Towards the molecular mechanism of respiratory complex i
    • Hirst, J. (2010) Towards the molecular mechanism of respiratory complex I. Biochem. J. 425, 327-339.
    • (2010) Biochem. J. , vol.425 , pp. 327-339
    • Hirst, J.1
  • 2
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M. P. (2009) How mitochondria produce reactive oxygen species. Biochem. J. 417, 1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 3
    • 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, 441-447.
    • (2010) Nature , vol.465 , pp. 441-447
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 4
    • 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
  • 5
    • 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
  • 6
    • 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
  • 7
    • 12844249400 scopus 로고    scopus 로고
    • Characterization of the iron-sulfur cluster N7 (N1c) in the subunit NuoG of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli
    • DOI 10.1074/jbc.M410377200
    • Nakamaru-Ogiso, E., Yano, T., Yagi, T., and Ohnishi, T. (2005) Characterization of the iron-sulfur cluster N7 (N1c) in the subunit NuoG of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli. J. Biol. Chem. 280, 301-307. (Pubitemid 40164993)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 301-307
    • Nakamaru-Ogiso, E.1    Yano, T.2    Yagi, T.3    Ohnishi, T.4
  • 8
    • 50149089377 scopus 로고    scopus 로고
    • Reduction of the iron-sulfur clusters in mitochondrial NADH:ubiquinone oxidoreductase (complex I) by EuII-DTPA, a very low potential reductant
    • Reda, T., Barker, C. D., and Hirst, J. (2008) Reduction of the iron-sulfur clusters in mitochondrial NADH:ubiquinone oxidoreductase (complex I) by EuII-DTPA, a very low potential reductant. Biochemistry 47, 8885-8893.
    • (2008) Biochemistry , vol.47 , pp. 8885-8893
    • Reda, T.1    Barker, C.D.2    Hirst, J.3
  • 9
    • 76649102458 scopus 로고    scopus 로고
    • Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex i by double electron-electron resonance
    • Roessler, M. M., King, M. S., Robinson, A. J., Armstrong, F. A., Harmer, J., and Hirst, J. (2010) Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonance. Proc. Natl. Acad. Sci. U. S. A. 107, 1930-1935.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 1930-1935
    • Roessler, M.M.1    King, M.S.2    Robinson, A.J.3    Armstrong, F.A.4    Harmer, J.5    Hirst, J.6
  • 10
    • 50949130428 scopus 로고    scopus 로고
    • Were there any ?misassignments? among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)? Biochim
    • Ohnishi, T., and Nakamaru-Ogiso, E. (2008) Were there any ?misassignments? among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)? Biochim. Biophys. Acta 1777, 703-710.
    • (2008) Biophys. Acta , vol.1777 , pp. 703-710
    • Ohnishi, T.1    Nakamaru-Ogiso, E.2
  • 11
    • 34547917597 scopus 로고    scopus 로고
    • Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH:quinone oxidoreductase
    • DOI 10.1073/pnas.0705593104
    • Yakovlev, G., Reda, T., and Hirst, J. (2007) Reevaluating the relationship between EPR spectra and enzyme structure for the ironsulfur clusters in NADH:quinone oxidoreductase. Proc. Natl. Acad. Sci. U. S. A. 104, 12720-12725. (Pubitemid 47255221)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.31 , pp. 12720-12725
    • Yakovlev, G.1    Reda, T.2    Hirst, J.3
  • 12
    • 0029112808 scopus 로고
    • Expression and characterization of the 66-kilodalton (NQO3) ironsulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Yano, T., Yagi, T., Sled, V. D., and Ohnishi, T. (1995) Expression and characterization of the 66-kilodalton (NQO3) ironsulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. J. Biol. Chem. 270, 18264-18270.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18264-18270
    • Yano, T.1    Yagi, T.2    Sled, V.D.3    Ohnishi, T.4
  • 13
    • 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 mitochondria l 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
  • 14
    • 13444259531 scopus 로고    scopus 로고
    • Characterisation of the ?μH+-sensitive ubisemiquinione species (SQNf) and the interaction with cluster N2: New insight into the energy-coupled electron transfer in complex I
    • DOI 10.1021/bi048132i
    • Yano, T., Dunham, W. R., and Ohnishi, T. (2005) Characterisation of the ?μH+-sensitive ubisemiquinione species (SQNf) and the interaction with cluster N2: New insight into the energy-coupled electron transfer in complex I. Biochemistry 44, 1744-1754. (Pubitemid 40204415)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1744-1754
    • Yano, T.1    Dunham, W.R.2    Ohnishi, T.3
  • 15
    • 0026495482 scopus 로고
    • On the stoichiometry of the iron-sulfur clusters in mitochondrial NADH:ubiquinone oxidoreductase
    • van Belzen, R., de Jong, A. M. P., and Albracht, S. P. J. (1992) On the stoichiometry of the iron-sulfur clusters in mitochondrial NADH:ubiquinone oxidoreductase. Eur. J. Biochem. 209, 1019-1022.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 1019-1022
    • Van Belzen, R.1    De Jong, A.M.P.2    Albracht, S.P.J.3
  • 16
    • 66349089690 scopus 로고    scopus 로고
    • New pulsed EPR methods and their application to characterize mitochondrial complex i
    • Maly, T., Zwicker, K., Cernescu, A., Brandt, U., and Prisner, T. F. (2009) New pulsed EPR methods and their application to characterize mitochondrial complex I. Biochim. Biophys. Acta 1787, 584-592.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 584-592
    • Maly, T.1    Zwicker, K.2    Cernescu, A.3    Brandt, U.4    Prisner, T.F.5
  • 17
    • 0037844859 scopus 로고    scopus 로고
    • Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans
    • DOI 10.1074/jbc.M212275200
    • Yano, T., Sklar, J., Nakamaru-Ogiso, E., Takahashi, Y., Yagi, T., and Ohnishi, T. (2003) Characterization of cluster N5 as a fastrelaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans. J. Biol. Chem. 278, 15514-15522. (Pubitemid 36799658)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.18 , pp. 15514-15522
    • Yano, T.1    Sklar, J.2    Nakamaru-Ogiso, E.3    Takahashi, Y.4    Yagi, T.5    Ohnishi, T.6
  • 18
    • 0037031281 scopus 로고    scopus 로고
    • Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH:Ubiquinone oxidoreductase (complex I)
    • DOI 10.1021/bi026026f
    • Zu, Y., Di Bernardo, S., Yagi, T., and Hirst, J. (2002) Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH:ubiquinone oxidoreductase (complex I). Biochemistry 41, 10056-10069. (Pubitemid 34839751)
    • (2002) Biochemistry , vol.41 , Issue.31 , pp. 10056-10069
    • Zu, Y.1    Di Bernardo, S.2    Yagi, T.3    Hirst, J.4
  • 19
    • 33947370457 scopus 로고    scopus 로고
    • + reduction from protein film voltammetry
    • DOI 10.1021/bi061988y
    • Barker, C. D., Reda, T., and Hirst, J. (2007) The flavoprotein subcomplex of complex I (NADH:ubiquinone oxidoreductase) from bovine heart mitochondria: Insights into the mechanisms of NADH oxidation and NAD+ reduction from protein film voltammetry. Biochemistry 46, 3454-3464. (Pubitemid 46449163)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3454-3464
    • Barker, C.D.1    Reda, T.2    Hirst, J.3
  • 20
    • 0029075136 scopus 로고
    • Isolation and characterisation of the proton-translocating NADH-ubiquinone oxidoreductase from Escherichia coli
    • Leif, H., Sled, V. D., Ohnishi, T., Weiss, H., and Friedrich, T. (1995) Isolation and characterisation of the proton-translocating NADH-ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230, 538-548.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 21
    • 0019877322 scopus 로고
    • Iron sulfur N-1 clusters studied in NADH-ubiquinone oxidoreductase and in soluble NADH dehydrogenase
    • Ohnishi, T., Blum, H., Galante, Y. M., and Hatefi, Y. (1981) Iron sulfur N-1 clusters studied in NADH-ubiquinone oxidoreductase and in soluble NADH dehydrogenase. J. Biol. Chem. 256, 9216-9220.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9216-9220
    • Ohnishi, T.1    Blum, H.2    Galante, Y.M.3    Hatefi, Y.4
  • 22
    • 0019324533 scopus 로고
    • An analysis of some thermodynamic properties of iron-sulphur centres in site i of mitochondria
    • Ingledew, W. J., and Ohnishi, T. (1980) An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria. Biochem. J. 186, 111-117.
    • (1980) Biochem. J. , vol.186 , pp. 111-117
    • Ingledew, W.J.1    Ohnishi, T.2
  • 24
    • 0017227082 scopus 로고
    • Studies on the mechanism of site i energy conservation
    • Ohnishi, T. (1976) Studies on the mechanism of site I energy conservation. Eur. J. Biochem. 64, 91-103.
    • (1976) Eur. J. Biochem. , vol.64 , pp. 91-103
    • Ohnishi, T.1
  • 25
    • 0016687657 scopus 로고
    • Thermodynamic and EPR characterization of iron-sulfur centers in the NADH-ubiquinone oxidoreductase segment of the respiratory chain in pigeon heart
    • Ohnishi, T. (1975) Thermodynamic and EPR characterization of iron-sulfur centers in the NADH-ubiquinone oxidoreductase segment of the respiratory chain in pigeon heart. Biochim. Biophys. Acta 387, 475-490.
    • (1975) Biochim. Biophys. Acta , vol.387 , pp. 475-490
    • Ohnishi, T.1
  • 26
    • 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
  • 27
    • 33749184515 scopus 로고    scopus 로고
    • Electron tunneling chains of mitochondria
    • DOI 10.1016/j.bbabio.2006.04.015, PII S0005272806001083, Mitochondria: from Molecular Insight to Physiology and Pathology
    • Moser, C. C., Farid, T. A., Chobot, S. E., and Dutton, P. L. (2006) Electron tunneling chains of mitochondria. Biochim. Biophys. Acta 1757, 1096-1109. (Pubitemid 44472548)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.9-10 , pp. 1096-1109
    • Moser, C.C.1    Farid, T.A.2    Chobot, S.E.3    Dutton, P.L.4
  • 28
    • 67649958261 scopus 로고    scopus 로고
    • Electrostatics of the FeS clusters in respiratory complex i
    • Couch, V. A., Medvedev, E. S., and Stuchebrukhov, A. A. (2009) Electrostatics of the FeS clusters in respiratory complex I. Biochim. Biophys. Acta 1787, 1266-1271.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1266-1271
    • Couch, V.A.1    Medvedev, E.S.2    Stuchebrukhov, A.A.3
  • 29
    • 67650563880 scopus 로고    scopus 로고
    • Aromatic amino acids as stepping stones in charge transfer in respiratory complex I: An unusual mechanism deduced from atomistic theory and bioinformatics
    • Wittekindt, C., Schwarz, M., Friedrich, T., and Koslowski, T. (2009) Aromatic amino acids as stepping stones in charge transfer in respiratory complex I: an unusual mechanism deduced from atomistic theory and bioinformatics. J. Am. Chem. Soc. 131, 8134-8140.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8134-8140
    • Wittekindt, C.1    Schwarz, M.2    Friedrich, T.3    Koslowski, T.4
  • 30
    • 77954761571 scopus 로고    scopus 로고
    • Determination of the intrinsic redox potentials of FeS centers of respiratory complex i from experimental titration curves
    • Medvedev, E. S., Couch, V. A., and Stuchebrukhov, A. A. (2010) Determination of the intrinsic redox potentials of FeS centers of respiratory complex I from experimental titration curves. Biochim. Biophys. Acta 1797, 1665-1671.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1665-1671
    • Medvedev, E.S.1    Couch, V.A.2    Stuchebrukhov, A.A.3
  • 32
    • 77953810633 scopus 로고    scopus 로고
    • The flitting of electrons in complex I: A stochastic approach
    • Ransac, S., Arnarez, C., and Mazat, J. P. (2010) The flitting of electrons in complex I: a stochastic approach. Biochim. Biophys. Acta 1797, 641-648.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 641-648
    • Ransac, S.1    Arnarez, C.2    Mazat, J.P.3
  • 33
    • 0035795187 scopus 로고    scopus 로고
    • Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica
    • DOI 10.1016/S0005-2728(00)00266-8, PII S0005272800002668
    • Kashani-Poor, N., Kerscher, S., Zickermann, V., and Brandt, U. (2001) Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta 1504, 363-370. (Pubitemid 32201908)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1504 , Issue.2-3 , pp. 363-370
    • Kashani-Poor, N.1    Kerscher, S.2    Zickermann, V.3    Brandt, U.4
  • 34
    • 28244435454 scopus 로고    scopus 로고
    • Proton pumping by complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica reconstituted into proteoliposomes
    • DOI 10.1016/j.bbabio.2005.10.001, PII S000527280500232X
    • Dröse, S., Galkin, A., and Brandt, U. (2005) Proton pumping by complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica reconstituted into proteoliposomes. Biochim. Biophys. Acta 1710, 87-95. (Pubitemid 41714004)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1710 , Issue.2-3 , pp. 87-95
    • Drose, S.1    Galkin, A.2    Brandt, U.3
  • 35
    • 68749112864 scopus 로고    scopus 로고
    • The respiratory complexes i from the mitochondria of two Pichia species
    • Bridges, H. R., Grgic, L., Harbour, M. E., and Hirst, J. (2009) The respiratory complexes I from the mitochondria of two Pichia species. Biochem. J. 422, 151-159.
    • (2009) Biochem. J. , vol.422 , pp. 151-159
    • Bridges, H.R.1    Grgic, L.2    Harbour, M.E.3    Hirst, J.4
  • 36
    • 0034777015 scopus 로고    scopus 로고
    • Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration
    • Pieroni, L., Khalil, L., Charlotte, F., Poynard, T., Piton, A., Hainque, B., and Imbert-Bismut, F. (2001) Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration. Clin. Chem. 47, 2059-2061. (Pubitemid 33010732)
    • (2001) Clinical Chemistry , vol.47 , Issue.11 , pp. 2059-2061
    • Pieroni, L.1    Khalil, L.2    Charlotte, F.3    Poynard, T.4    Piton, A.5    Hainque, B.6    Imbert-Bismut, F.7
  • 40
    • 79951517083 scopus 로고    scopus 로고
    • Optimized implementations of rational approximations for the Voigt and complex error function
    • Schreier, F. (2011) Optimized implementations of rational approximations for the Voigt and complex error function. J. Quant. Spectrosc. Radiat. Transfer 112, 1010-1025.
    • (2011) J. Quant. Spectrosc. Radiat. Transfer , vol.112 , pp. 1010-1025
    • Schreier, F.1
  • 41
  • 45
    • 0015528120 scopus 로고
    • Mössbauer parameters of putidaredoxin and its selenium analog
    • Münck, E., Debrunner, P. G., Tsibris, J. C. M., and Gunsalus, I. C. (1972) Mössbauer parameters of putidaredoxin and its selenium analog. Biochemistry 11, 855-863.
    • (1972) Biochemistry , vol.11 , pp. 855-863
    • Münck, E.1    Debrunner, P.G.2    Tsibris, J.C.M.3    Gunsalus, I.C.4
  • 47
    • 0017729558 scopus 로고
    • The number of Fe atoms in the iron-sulphur centers of the respiratory chain
    • Albracht, S. P. J., and Subramanian, J. (1977) The number of Fe atoms in the iron-sulphur centers of the respiratory chain. Biochim. Biophys. Acta 462, 36-48. (Pubitemid 8232605)
    • (1977) Biochimica et Biophysica Acta , vol.462 , Issue.1 , pp. 36-48
    • Albracht, S.P.J.1    Subramanian, J.2
  • 48
    • 0016249116 scopus 로고
    • Spectroscopic studies on two-iron ferredoxins
    • Sands, R. H., and Dunham, W. R. (1975) Spectroscopic studies on two-iron ferredoxins. Q. Rev. Biophys. 7, 443-504.
    • (1975) Q. Rev. Biophys. , vol.7 , pp. 443-504
    • Sands, R.H.1    Dunham, W.R.2
  • 49
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • DOI 10.1126/science.277.5326.653
    • Beinert, H., Holm, R. H., and Münck, E. (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 277, 653-659. (Pubitemid 27373905)
    • (1997) Science , vol.277 , Issue.5326 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 50
    • 0033910009 scopus 로고    scopus 로고
    • Structure and dynamics of biomolecules studied by Mössbauer spectroscopy
    • Schünemann, V., and Winkler, H. (2000) Structure and dynamics of biomolecules studied by Mössbauer spectroscopy. Rep. Prog. Phys. 63, 263-353.
    • (2000) Rep. Prog. Phys. , vol.63 , pp. 263-353
    • Schünemann, V.1    Winkler, H.2
  • 51
    • 0032263876 scopus 로고    scopus 로고
    • Iron - Sulfur clusters and their electronic and magnetic properties
    • PII S0010854598001556
    • Mouesca, J. M., and Lamotte, B. (1998) Iron-sulfur clusters and their electronic and magnetic properties. Coord. Chem. Rev. 180, 1573-1614. (Pubitemid 128452093)
    • (1998) Coordination Chemistry Reviews , vol.178-180 , Issue.PART 2 , pp. 1573-1614
    • Mouesca, J.-M.1    Lamotte, B.2
  • 52
    • 0017902720 scopus 로고
    • Interpretation of the Mossbauer spectra of the four-iron ferredoxin from Bacillus stearothermophilus
    • Middleton, P., Dickson, D. P. E., Johnson, C. E., and Rush, J. D. (1978) Interpretation of the Mössbauer spectra of the four-iron ferredoxin from Bacillus stearothermophilis. Eur. J. Biochem. 88, 135-141. (Pubitemid 8367848)
    • (1978) European Journal of Biochemistry , vol.88 , Issue.1 , pp. 135-141
    • Middleton, P.1    Dickson, D.P.E.2    Johnson, C.E.3    Rush, J.D.4
  • 54
    • 0030613554 scopus 로고    scopus 로고
    • Mössbauer study of 4-hydroxybutyryl-CoA dehydratase
    • Müh, U., Buckel, W., and Bill, E. (1997) Mössbauer study of 4-hydroxybutyryl-CoA dehydratase. Eur. J. Biochem. 248, 380-384.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 380-384
    • Müh, U.1    Buckel, W.2    Bill, E.3
  • 55
    • 0023030622 scopus 로고
    • Spectroscopic characterization of the number and type of iron-sulfur clusters in NADH: Ubiquinone oxidoreductase
    • Kowal, A. T., Morningstar, J. E., Johnson, M. K., Ramsay, R. R., and Singer, T. P. (1986) Spectroscopic characterization of the number and type of iron-sulfur clusters in NADH:ubiquinone oxidoreductase. J. Biol. Chem. 261, 9239-9245. (Pubitemid 17218200)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.20 , pp. 9239-9245
    • Kowal, A.T.1    Morningstar, J.E.2    Johnson, M.K.3
  • 56
    • 40549126917 scopus 로고    scopus 로고
    • Electrostatic interactions between FeS clusters in NADH:Ubiquinone oxidoreductase (complex I) from Escherichia coli
    • DOI 10.1021/bi702063t
    • Euro, L., Bloch, D. A., Wikström, M., Verkhovsky, M. I., and Verkhovskaya, M. (2008) Electrostatic interactions between FeS clusters in NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry 47, 3185-3193. (Pubitemid 351364911)
    • (2008) Biochemistry , vol.47 , Issue.10 , pp. 3185-3193
    • Euro, L.1    Bloch, D.A.2    Wikstrom, M.3    Verkhovsky, M.I.4    Verkhovskaya, M.5
  • 59
    • 84856816500 scopus 로고    scopus 로고
    • Ph.D. Thesis, Cambridge University
    • King, M. S. (2010) Ph.D. Thesis Cambridge University.
    • (2010)
    • King, M.S.1
  • 60
    • 0035968167 scopus 로고    scopus 로고
    • A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex i
    • Kashani-Poor, N., Zwicker, K., Kerscher, S., and Brandt, U. (2001) A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I. J. Biol. Chem. 276, 24082-24087.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24082-24087
    • Kashani-Poor, N.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 64
    • 33645459555 scopus 로고    scopus 로고
    • Kinetic performance and energy profile in a roller coaster electron transfer chain: A study of modified tetraheme-reaction center constructs
    • Alric, J., Lavergne, J., Rappaport, F., Verméglio, A., Matsuura, K., Shimada, K., and Nagashima, K. V. P. (2006) Kinetic performance and energy profile in a roller coaster electron transfer chain: a study of modified tetraheme-reaction center constructs. J. Am. Chem. Soc. 128, 4136-4145.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4136-4145
    • Alric, J.1    Lavergne, J.2    Rappaport, F.3    Verméglio, A.4    Matsuura, K.5    Shimada, K.6    Nagashima, K.V.P.7
  • 65
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X. X., and Dutton, P. L. (1999) Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.X.3    Dutton, P.L.4
  • 68
    • 0013966412 scopus 로고
    • Studies of photosynthesis using a pulsed laser I. Temperature dependence of cytochrome oxidation rate in Chromatium. Evidence for tunneling
    • DeVault, D., and Chance, B. (1966) Studies of photosynthesis using a pulsed laser. I. Temperature dependence of cytochrome oxidation rate in Chromatium. Evidence for tunneling. Biophys. J. 6, 825-847.
    • (1966) Biophys. J. , vol.6 , pp. 825-847
    • Devault, D.1    Chance, B.2
  • 69
    • 30144445462 scopus 로고    scopus 로고
    • Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondrial
    • DOI 10.1021/bi051809x
    • Sharpley, M. S., Shannon, R. J., Draghi, F., and Hirst, J. (2006) Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria. Biochemistry 45, 241-248. (Pubitemid 43054102)
    • (2006) Biochemistry , vol.45 , Issue.1 , pp. 241-248
    • Sharpley, M.S.1    Shannon, R.J.2    Draghi, F.3    Hirst, J.4
  • 70
    • 79958806288 scopus 로고    scopus 로고
    • Dynamics of the [4Fe-4S] cluster in Pyrococcus furiosus D14C ferredoxin via nuclear resonance vibrational and resonance Raman spectroscopies, force field simulations, and density functional theory calculations
    • Mitra, D., Pelmenschikov, V., Guo, Y., Case, D. A., Wang, H., Dong, W., Tan, M.-L., Ichiye, T., Jenney, F. E., Adams, M. W. W., Yoda, Y., Zhao, J., and Cramer, S. P. (2011) Dynamics of the [4Fe-4S] cluster in Pyrococcus furiosus D14C ferredoxin via nuclear resonance vibrational and resonance Raman spectroscopies, force field simulations, and density functional theory calculations. Biochemistry 50, 5220-5235.
    • (2011) Biochemistry , vol.50 , pp. 5220-5235
    • Mitra, D.1    Pelmenschikov, V.2    Guo, Y.3    Case, D.A.4    Wang, H.5    Dong, W.6    Tan, M.-L.7    Ichiye, T.8    Jenney, F.E.9    Adams, M.W.W.10    Yoda, Y.11    Zhao, J.12    Cramer, S.P.13


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