메뉴 건너뛰기




Volumn 16, Issue 6, 2015, Pages 375-388

A giant molecular proton pump: Structure and mechanism of respiratory complex I

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; PROTON PUMP; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); BACTERIAL PROTEIN; CYTOCHROME C OXIDASE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84930041923     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3997     Document Type: Review
Times cited : (388)

References (90)
  • 2
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell, P. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191, 144-148 (1961).
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 3
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J. P., Leslie, A. G., Lutter, R. & Walker, J. E. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621-628 (1994).
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 5
    • 0028890031 scopus 로고
    • Structure at 2.8 a resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376, 660-669 (1995).
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 6
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A
    • Tsukihara, T. et al. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Science 272, 1136-1144 (1996).
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1
  • 7
    • 0032479524 scopus 로고    scopus 로고
    • Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex
    • Iwata, S. et al. Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex. Science 281, 64-71 (1998).
    • (1998) Science , vol.281 , pp. 64-71
    • Iwata, S.1
  • 8
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein complex II
    • Sun, F. et al. Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121, 1043-1057 (2005).
    • (2005) Cell , vol.121 , pp. 1043-1057
    • Sun, F.1
  • 9
    • 84874352529 scopus 로고    scopus 로고
    • Crystal structure of the entire respiratory complex i
    • Baradaran, R., Berrisford, J. M., Minhas, G. S. & Sazanov, L. A. Crystal structure of the entire respiratory complex I. Nature 494, 443-448 (2013).
    • (2013) Nature , vol.494 , pp. 443-448
    • Baradaran, R.1    Berrisford, J.M.2    Minhas, G.S.3    Sazanov, L.A.4
  • 10
    • 84864689276 scopus 로고    scopus 로고
    • A review of the binding-change mechanism for proton-Translocating transhydrogenase
    • Jackson, J. B. A review of the binding-change mechanism for proton-Translocating transhydrogenase. Biochim. Biophys. Acta 1817, 1839-1846 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1839-1846
    • Jackson, J.B.1
  • 12
    • 0028339522 scopus 로고
    • Proton-Translocating transhydrogenase and NAD-And NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria
    • Sazanov, L. A. & Jackson, J. B. Proton-Translocating transhydrogenase and NAD-And NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria. FEBS Lett. 344, 109-116 (1994).
    • (1994) FEBS Lett. , vol.344 , pp. 109-116
    • Sazanov, L.A.1    Jackson, J.B.2
  • 13
    • 0028269382 scopus 로고
    • Catalytic sector of complex i (NADH:ubiquinone oxidoreductase): Subunit stoichiometry and substrate-induced conformation changes
    • Belogrudov, G. & Hatefi, Y. Catalytic sector of complex I (NADH:ubiquinone oxidoreductase): subunit stoichiometry and substrate-induced conformation changes. Biochemistry 33, 4571-4576 (1994).
    • (1994) Biochemistry , vol.33 , pp. 4571-4576
    • Belogrudov, G.1    Hatefi, Y.2
  • 14
    • 2542421934 scopus 로고    scopus 로고
    • Substrate-induced conformational change in bacterial complex i
    • Mamedova, A. A., Holt, P. J., Carroll, J. & Sazanov, L. A. Substrate-induced conformational change in bacterial complex I. J. Biol. Chem. 279, 23830-23836 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 23830-23836
    • Mamedova, A.A.1    Holt, P.J.2    Carroll, J.3    Sazanov, L.A.4
  • 15
    • 52949114593 scopus 로고    scopus 로고
    • Chemical and NADH-induced ROS-dependent cross-linking between subunits of complex i from Escherichia coli and
    • Berrisford, J. M., Thompson, C. J. & Sazanov, L. A. Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of complex I from Escherichia coli and Thermus thermophilus. Biochemistry 47, 10262-10270 (2008).
    • (2008) Thermus Thermophilus. Biochemistry , vol.47 , pp. 10262-10270
    • Berrisford, J.M.1    Thompson, C.J.2    Sazanov, L.A.3
  • 16
    • 34547096741 scopus 로고    scopus 로고
    • Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex i
    • Baranova, E. A., Morgan, D. J. & Sazanov, L. A. Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I. J. Struct. Biol. 159, 238-242 (2007).
    • (2007) J. Struct. Biol. , vol.159 , pp. 238-242
    • Baranova, E.A.1    Morgan, D.J.2    Sazanov, L.A.3
  • 17
    • 0242322000 scopus 로고    scopus 로고
    • The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I: Implications for the mechanism of proton pumping
    • Holt, P. J., Morgan, D. J. & Sazanov, L. A. The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I: implications for the mechanism of proton pumping. J. Biol. Chem. 278, 43114-43120 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 43114-43120
    • Holt, P.J.1    Morgan, D.J.2    Sazanov, L.A.3
  • 18
    • 0034691280 scopus 로고    scopus 로고
    • Resolution of the membrane domain of bovine complex i into subcomplexes: Implications for the structural organization of the enzyme
    • Sazanov, L. A., Peak-Chew, S. Y., Fearnley, I. M. & Walker, J. E. Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme. Biochemistry 39, 7229-7235 (2000).
    • (2000) Biochemistry , vol.39 , pp. 7229-7235
    • Sazanov, L.A.1    Peak-Chew, S.Y.2    Fearnley, I.M.3    Walker, J.E.4
  • 19
    • 0034665878 scopus 로고    scopus 로고
    • Cryo-electron crystallography of two sub-complexes of bovine complex i reveals the relationship between the membrane and peripheral arms
    • Sazanov, L. A. & Walker, J. E. Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms. J. Mol. Biol. 302, 455-464 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 455-464
    • Sazanov, L.A.1    Walker, J.E.2
  • 20
    • 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. & Sazanov, L. A. Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochim. Biophys. Acta 1777, 711-718 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 711-718
    • Morgan, D.J.1    Sazanov, L.A.2
  • 21
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice
    • Grigorieff, N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice. J. Mol. Biol. 277, 1033-1046 (1998).
    • (1998) J. Mol. Biol. , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 22
    • 0032512616 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Guenebaut, V., Schlitt, A., Weiss, H., Leonard, K. & Friedrich, T. Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol. 276, 105-112 (1998).
    • (1998) J. Mol. Biol. , vol.276 , pp. 105-112
    • Guenebaut, V.1    Schlitt, A.2    Weiss, H.3    Leonard, K.4    Friedrich, T.5
  • 23
    • 79953131437 scopus 로고    scopus 로고
    • Evolution of respiratory complex I: Supernumerary subunits are present in the alpha-proteobacterial enzyme
    • Yip, C. Y., Harbour, M. E., Jayawardena, K., Fearnley, I. M. & Sazanov, L. A. Evolution of respiratory complex I: 'supernumerary' subunits are present in the alpha-proteobacterial enzyme. J. Biol. Chem. 286, 5023-5033 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 5023-5033
    • Yip, C.Y.1    Harbour, M.E.2    Jayawardena, K.3    Fearnley, I.M.4    Sazanov, L.A.5
  • 24
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • Brandt, U. Energy converting NADH:quinone oxidoreductase (complex I). Annu. Rev. Biochem. 75, 69-92 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 69-92
    • Brandt, U.1
  • 25
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker, J. E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25, 253-324 (1992).
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 27
    • 84915761829 scopus 로고    scopus 로고
    • Architecture of mammalian respiratory complex i
    • Vinothkumar, K. R., Zhu, J. & Hirst, J. Architecture of mammalian respiratory complex I. Nature 515, 80-84 (2014).
    • (2014) Nature , vol.515 , pp. 80-84
    • Vinothkumar, K.R.1    Zhu, J.2    Hirst, J.3
  • 28
    • 77953136730 scopus 로고    scopus 로고
    • Small single transmembrane domain (STMD) proteins organize the hydrophobic subunits of large membrane protein complexes
    • Zickermann, V., Angerer, H., Ding, M. G., Nubel, E. & Brandt, U. Small single transmembrane domain (STMD) proteins organize the hydrophobic subunits of large membrane protein complexes. FEBS Lett. 584, 2516-2525 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 2516-2525
    • Zickermann, V.1    Angerer, H.2    Ding, M.G.3    Nubel, E.4    Brandt, U.5
  • 29
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex i
    • Hunte, C., Zickermann, V. & Brandt, U. Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 329, 448-451 (2010).
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 30
    • 80052097536 scopus 로고    scopus 로고
    • Respiratory complex I: 'steam engine' of the cell?
    • Efremov, R. G. & Sazanov, L. A. Respiratory complex I: 'steam engine' of the cell? Curr. Opin. Struct. Biol. 21, 532-540 (2011).
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 532-540
    • Efremov, R.G.1    Sazanov, L.A.2
  • 31
    • 0026484793 scopus 로고
    • Conservation of sequences of subunits of mitochondrial complex i and their relationships with other proteins
    • Fearnley, I. M. & Walker, J. E. Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins. Biochim. Biophys. Acta 1140, 105-134 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 105-134
    • Fearnley, I.M.1    Walker, J.E.2
  • 32
    • 84922479528 scopus 로고    scopus 로고
    • Mechanistic insight from the crystal structure of mitochondrial complex i
    • Zickermann, V. et al. Mechanistic insight from the crystal structure of mitochondrial complex I. Science 347, 44-49 (2015).
    • (2015) Science , vol.347 , pp. 44-49
    • Zickermann, V.1
  • 33
    • 70350351403 scopus 로고    scopus 로고
    • Structural basis for the mechanism of respiratory complex i
    • Berrisford, J. M. & Sazanov, L. A. Structural basis for the mechanism of respiratory complex I. J. Biol. Chem. 284, 29773-29783 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 29773-29783
    • Berrisford, J.M.1    Sazanov, L.A.2
  • 34
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex i from
    • Sazanov, L. A. & Hinchliffe, P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311, 1430-1436 (2006).
    • (2006) Thermus Thermophilus. Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 35
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex i
    • Efremov, R. G. & Sazanov, L. A. Structure of the membrane domain of respiratory complex I. Nature 476, 414-420 (2011).
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 36
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex i
    • Efremov, R. G., Baradaran, R. & Sazanov, L. A. The architecture of respiratory complex I. Nature 465, 441-445 (2010).
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 37
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • Sazanov, L. A. Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry 46, 2275-2288 (2007).
    • (2007) Biochemistry , vol.46 , pp. 2275-2288
    • Sazanov, L.A.1
  • 38
    • 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, 186-206 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 39
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X. & Dutton, P. L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402, 47-52 (1999).
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 40
    • 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
    • Pohl, T. et al. 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 (2007).
    • (2007) Biochemistry , vol.46 , pp. 6588-6596
    • Pohl, T.1
  • 41
    • 0037010862 scopus 로고    scopus 로고
    • Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters
    • Mathiesen, C. & Hagerhall, C. Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters. Biochim. Biophys. Acta 1556, 121-132 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 121-132
    • Mathiesen, C.1    Hagerhall, C.2
  • 43
    • 34447637751 scopus 로고    scopus 로고
    • Discontinuous membrane helices in transport proteins and their correlation with function
    • Screpanti, E. & Hunte, C. Discontinuous membrane helices in transport proteins and their correlation with function. J. Struct. Biol. 159, 261-267 (2007).
    • (2007) J. Struct. Biol. , vol.159 , pp. 261-267
    • Screpanti, E.1    Hunte, C.2
  • 44
    • 78349305451 scopus 로고    scopus 로고
    • Evolutionary origin of a secondary structure: P-helices as cryptic but widespread insertional variations of a-helices that enhance protein functionality
    • Cooley, R. B., Arp, D. J. & Karplus, P. A. Evolutionary origin of a secondary structure: p-helices as cryptic but widespread insertional variations of a-helices that enhance protein functionality. J. Mol. Biol. 404, 232-246 (2010).
    • (2010) J. Mol. Biol. , vol.404 , pp. 232-246
    • Cooley, R.B.1    Arp, D.J.2    Karplus, P.A.3
  • 45
    • 84864659415 scopus 로고    scopus 로고
    • The coupling mechanism of respiratory complex i-A structural and evolutionary perspective
    • Efremov, R. G. & Sazanov, L. A. The coupling mechanism of respiratory complex I-A structural and evolutionary perspective. Biochim. Biophys. Acta 1817, 1785-1795 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1785-1795
    • Efremov, R.G.1    Sazanov, L.A.2
  • 46
    • 0032490104 scopus 로고    scopus 로고
    • Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) and the pseudo-reversible active/inactive enzyme transition
    • Vinogradov, A. D. Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) and the pseudo-reversible active/inactive enzyme transition. Biochim. Biophys. Acta 1364, 169-185 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 169-185
    • Vinogradov, A.D.1
  • 49
    • 0025349462 scopus 로고
    • Coupling site i and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles
    • Kotlyar, A. B., Sled, V. D., Burbaev, D. S., Moroz, I. A. & Vinogradov, A. D. Coupling site I and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles. FEBS Lett. 264, 17-20 (1990).
    • (1990) FEBS Lett. , vol.264 , pp. 17-20
    • Kotlyar, A.B.1    Sled, V.D.2    Burbaev, D.S.3    Moroz, I.A.4    Vinogradov, A.D.5
  • 50
    • 84856917379 scopus 로고    scopus 로고
    • Mossbauer spectroscopy on respiratory complex I: The iron-sulfur cluster ensemble in the NADH-reduced enzyme is partially oxidized
    • Bridges, H. R., Bill, E. & Hirst, J. Mossbauer spectroscopy on respiratory complex I: the iron-sulfur cluster ensemble in the NADH-reduced enzyme is partially oxidized. Biochemistry 51, 149-158 (2012).
    • (2012) Biochemistry , vol.51 , pp. 149-158
    • Bridges, H.R.1    Bill, E.2    Hirst, J.3
  • 51
    • 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. et al. Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonance. Proc. Natl Acad. Sci. USA 107, 1930-1935 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1930-1935
    • Roessler, M.M.1
  • 52
    • 33750432874 scopus 로고    scopus 로고
    • Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5?-phosphosulfate reductase
    • Chartron, J. et al. Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5?-phosphosulfate reductase. J. Mol. Biol. 364, 152-169 (2006).
    • (2006) J. Mol. Biol. , vol.364 , pp. 152-169
    • Chartron, J.1
  • 54
    • 69249116947 scopus 로고    scopus 로고
    • Structure and mechanism of a Na+-independent amino acid transporter
    • Shaffer, P. L., Goehring, A., Shankaranarayanan, A. & Gouaux, E. Structure and mechanism of a Na+-independent amino acid transporter. Science 325, 1010-1014 (2009).
    • (2009) Science , vol.325 , pp. 1010-1014
    • Shaffer, P.L.1    Goehring, A.2    Shankaranarayanan, A.3    Gouaux, E.4
  • 55
    • 77957257818 scopus 로고    scopus 로고
    • Single site mutations in the hetero-oligomeric Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4 that affect Na+/H+ antiport activity, sodium exclusion, individual Mrp protein levels, or Mrp complex formation
    • Morino, M. et al. Single site mutations in the hetero-oligomeric Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4 that affect Na+/H+ antiport activity, sodium exclusion, individual Mrp protein levels, or Mrp complex formation. J. Biol. Chem. 285, 30942-30950 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 30942-30950
    • Morino, M.1
  • 56
    • 84885576596 scopus 로고    scopus 로고
    • A two-domain elevator mechanism for sodium/proton antiport
    • Lee, C. et al. A two-domain elevator mechanism for sodium/proton antiport. Nature 501, 573-577 (2013).
    • (2013) Nature , vol.501 , pp. 573-577
    • Lee, C.1
  • 57
    • 21744436321 scopus 로고    scopus 로고
    • Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH
    • Hunte, C. et al. Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH. Nature 435, 1197-1202 (2005).
    • (2005) Nature , vol.435 , pp. 1197-1202
    • Hunte, C.1
  • 58
    • 66249098083 scopus 로고    scopus 로고
    • Unlocking the molecular secrets of sodium-coupled transporters
    • Krishnamurthy, H., Piscitelli, C. L. & Gouaux, E. Unlocking the molecular secrets of sodium-coupled transporters. Nature 459, 347-355 (2009).
    • (2009) Nature , vol.459 , pp. 347-355
    • Krishnamurthy, H.1    Piscitelli, C.L.2    Gouaux, E.3
  • 59
    • 84886421872 scopus 로고    scopus 로고
    • Arginine oscillation explains Na+ independence in the substrate/product antiporter CaiT
    • Kalayil, S., Schulze, S. & Kuhlbrandt, W. Arginine oscillation explains Na+ independence in the substrate/product antiporter CaiT. Proc. Natl Acad. Sci. USA 110, 17296-17301 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 17296-17301
    • Kalayil, S.1    Schulze, S.2    Kuhlbrandt, W.3
  • 60
    • 84867275957 scopus 로고    scopus 로고
    • The deactive form of respiratory complex i from mammalian mitochondria is a Na+/H+ antiporter
    • Roberts, P. G. & Hirst, J. The deactive form of respiratory complex I from mammalian mitochondria is a Na+/H+ antiporter. J. Biol. Chem. 287, 34743-34751 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 34743-34751
    • Roberts, P.G.1    Hirst, J.2
  • 61
    • 0037072803 scopus 로고    scopus 로고
    • The respiratory complex i (NDH-1) from Klebsiella pneumoniae, a sodium pump
    • Gemperli, A. C., Dimroth, P. & Steuber, J. The respiratory complex I (NDH-1) from Klebsiella pneumoniae, a sodium pump. J. Biol. Chem. 277, 33811-33817 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 33811-33817
    • Gemperli, A.C.1    Dimroth, P.2    Steuber, J.3
  • 62
    • 0028972337 scopus 로고
    • Strange bedfellows: Interactions between acidic side-chains in proteins
    • Flocco, M. M. & Mowbray, S. L. Strange bedfellows: interactions between acidic side-chains in proteins. J. Mol. Biol. 254, 96-105 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 96-105
    • Flocco, M.M.1    Mowbray, S.L.2
  • 63
    • 84872332798 scopus 로고    scopus 로고
    • Energy-converting respiratory complex I: On the way to the molecular mechanism of the proton pump
    • Verkhovskaya, M. & Bloch, D. A. Energy-converting respiratory complex I: on the way to the molecular mechanism of the proton pump. Int. J. Biochem. Cell Biol. 45, 491-511 (2013).
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 491-511
    • Verkhovskaya, M.1    Bloch, D.A.2
  • 64
    • 84883180274 scopus 로고    scopus 로고
    • Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2)
    • Sato, M., Sinha, P. K., Torres-Bacete, J., Matsuno-Yagi, A. & Yagi, T. Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2). J. Biol. Chem. 288, 24705-24716 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 24705-24716
    • Sato, M.1    Sinha, P.K.2    Torres-Bacete, J.3    Matsuno-Yagi, A.4    Yagi, T.5
  • 65
    • 84900514379 scopus 로고    scopus 로고
    • Electrostatics hydration, and proton transfer dynamics in the membrane domain of respiratory complex i
    • Kaila, V. R., Wikstrom, M. & Hummer, G. Electrostatics, hydration, and proton transfer dynamics in the membrane domain of respiratory complex I. Proc. Natl Acad. Sci. USA 111, 6988-6993 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 6988-6993
    • Kaila, V.R.1    Wikstrom, M.2    Hummer, G.3
  • 67
    • 80051601805 scopus 로고    scopus 로고
    • A two-state stabilization-change mechanism for proton-pumping complex i
    • Brandt, U. A two-state stabilization-change mechanism for proton-pumping complex I. Biochim Biophys. Acta 1807, 1364-1369 (2011).
    • (2011) Biochim Biophys. Acta , vol.1807 , pp. 1364-1369
    • Brandt, U.1
  • 68
    • 84906343049 scopus 로고    scopus 로고
    • The mechanism of coupling between electron transfer and proton translocation in respiratory complex i
    • Sazanov, L. A. The mechanism of coupling between electron transfer and proton translocation in respiratory complex I. J. Bioenerg. Biomembr. 46, 247-253 (2014).
    • (2014) J. Bioenerg. Biomembr. , vol.46 , pp. 247-253
    • Sazanov, L.A.1
  • 69
    • 77957107068 scopus 로고    scopus 로고
    • A new hypothesis on the simultaneous direct and indirect proton pump mechanisms in NADH-quinone oxidoreductase (complex I)
    • Ohnishi, T., Nakamaru-Ogiso, E. & Ohnishi, S. T. A new hypothesis on the simultaneous direct and indirect proton pump mechanisms in NADH-quinone oxidoreductase (complex I). FEBS Lett. 584, 4131-4137 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 4131-4137
    • Ohnishi, T.1    Nakamaru-Ogiso, E.2    Ohnishi, S.T.3
  • 70
    • 51049093616 scopus 로고    scopus 로고
    • Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex i
    • Galkin, A. et al. Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I. J. Biol. Chem. 283, 20907-20913 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 20907-20913
    • Galkin, A.1
  • 71
    • 78649496491 scopus 로고    scopus 로고
    • The membrane subunit NuoL (ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex i
    • Nakamaru-Ogiso, E. et al. The membrane subunit NuoL (ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I. J. Biol. Chem. 285, 39070-39078 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 39070-39078
    • Nakamaru-Ogiso, E.1
  • 72
    • 80053201927 scopus 로고    scopus 로고
    • Structural contribution of C-Terminal segments of NuoL (ND5) and NuoM (ND4) subunits of complex i from
    • Torres-Bacete, J., Sinha, P. K., Matsuno-Yagi, A. & Yagi, T. Structural contribution of C-Terminal segments of NuoL (ND5) and NuoM (ND4) subunits of complex I from Escherichia coli. J. Biol. Chem. 286, 34007-34014 (2011).
    • (2011) Escherichia Coli. J. Biol. Chem. , vol.286 , pp. 34007-34014
    • Torres-Bacete, J.1    Sinha, P.K.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 73
    • 82155168224 scopus 로고    scopus 로고
    • Probing the mechanistic role of the long a-helix in subunit L of respiratory complex i from Escherichia coli by site-directed mutagenesis
    • Belevich, G., Knuuti, J., Verkhovsky, M. I., Wikstrom, M. & Verkhovskaya, M. Probing the mechanistic role of the long a-helix in subunit L of respiratory complex I from Escherichia coli by site-directed mutagenesis. Mol. Microbiol. 82, 1086-1095 (2011).
    • (2011) Mol. Microbiol. , vol.82 , pp. 1086-1095
    • Belevich, G.1    Knuuti, J.2    Verkhovsky, M.I.3    Wikstrom, M.4    Verkhovskaya, M.5
  • 74
    • 84858698111 scopus 로고    scopus 로고
    • Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex i
    • Steimle, S. et al. Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I. FEBS Lett. 586, 699-704 (2012).
    • (2012) FEBS Lett. , vol.586 , pp. 699-704
    • Steimle, S.1
  • 75
    • 0032490091 scopus 로고    scopus 로고
    • Human complex i defects in neurodegenerative diseases
    • Schapira, A. H. Human complex I defects in neurodegenerative diseases. Biochim. Biophys. Acta 1364, 261-270 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 261-270
    • Schapira, A.H.1
  • 76
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M. P. How mitochondria produce reactive oxygen species. Biochem. J. 417, 1-13 (2009).
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 77
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson, T. M. & Dawson, V. L. Molecular pathways of neurodegeneration in Parkinson's disease. Science 302, 819-822 (2003).
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 78
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria oxidants, and aging
    • Balaban, R. S., Nemoto, S. & Finkel, T. Mitochondria, oxidants, and aging. Cell 120, 483-495 (2005).
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 79
    • 0026702249 scopus 로고
    • Leber's hereditary optic neuropathy: A model for mitochondrial neurodegenerative diseases
    • Brown, M. D., Voljavec, A. S., Lott, M. T., MacDonald, I. & Wallace, D. C. Leber's hereditary optic neuropathy: a model for mitochondrial neurodegenerative diseases. FASEB J. 6, 2791-2799 (1992).
    • (1992) FASEB J. , vol.6 , pp. 2791-2799
    • Brown, M.D.1    Voljavec, A.S.2    Lott, M.T.3    MacDonald, I.4    Wallace, D.C.5
  • 80
    • 0025995774 scopus 로고
    • Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON)
    • Majander, A., Huoponen, K., Savontaus, M. L., Nikoskelainen, E. & Wikstrom, M. Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON). FEBS Lett. 292, 289-292 (1991).
    • (1991) FEBS Lett. , vol.292 , pp. 289-292
    • Majander, A.1    Huoponen, K.2    Savontaus, M.L.3    Nikoskelainen, E.4    Wikstrom, M.5
  • 81
    • 33846002728 scopus 로고    scopus 로고
    • A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth
    • Bonnet, S. et al. A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth. Cancer Cell 11, 37-51 (2007).
    • (2007) Cancer Cell , vol.11 , pp. 37-51
    • Bonnet, S.1
  • 82
    • 84873412963 scopus 로고    scopus 로고
    • Metformin and cancer: From the old medicine cabinet to pharmacological pitfalls and prospects
    • Emami Riedmaier, A., Fisel, P., Nies, A. T., Schaeffeler, E. & Schwab, M. Metformin and cancer: from the old medicine cabinet to pharmacological pitfalls and prospects. Trends Pharmacol. Sci. 34, 126-135 (2013).
    • (2013) Trends Pharmacol. Sci. , vol.34 , pp. 126-135
    • Emami Riedmaier, A.1    Fisel, P.2    Nies, A.T.3    Schaeffeler, E.4    Schwab, M.5
  • 83
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • Mitchell, P. The protonmotive Q cycle: a general formulation. FEBS Lett. 59, 137-139 (1975).
    • (1975) FEBS Lett. , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 84
    • 33748885262 scopus 로고    scopus 로고
    • Towards the mechanism of proton pumping by the haem-copper oxidases
    • Wikstrom, M. & Verkhovsky, M. I. Towards the mechanism of proton pumping by the haem-copper oxidases. Biochim. Biophys. Acta 1757, 1047-1051 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1047-1051
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 85
    • 2142697116 scopus 로고    scopus 로고
    • Energy-converting [NiFe] hydrogenases from archaea and extremophiles: Ancestors of complex i
    • Hedderich, R. Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I. J. Bioenerg. Biomembr. 36, 65-75 (2004).
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 65-75
    • Hedderich, R.1
  • 86
    • 79961032041 scopus 로고    scopus 로고
    • The evolution of respiratory chain complex i from a smaller last common ancestor consisting of 11 protein subunits
    • Moparthi, V. K. & Hagerhall, C. The evolution of respiratory chain complex I from a smaller last common ancestor consisting of 11 protein subunits. J. Mol. Evol. 72, 484-497 (2011).
    • (2011) J. Mol. Evol. , vol.72 , pp. 484-497
    • Moparthi, V.K.1    Hagerhall, C.2
  • 87
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex i of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • Friedrich, T. & Scheide, D. The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479, 1-5 (2000).
    • (2000) FEBS Lett. , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 88
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]-And [FeFe]-hydrogenases
    • Fontecilla-Camps, J. C., Volbeda, A., Cavazza, C. & Nicolet, Y. Structure/function relationships of [NiFe]-And [FeFe]-hydrogenases. Chem. Rev. 107, 4273-4303 (2007).
    • (2007) Chem. Rev. , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 89
    • 84863955498 scopus 로고    scopus 로고
    • Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM
    • Baker, L. A., Watt, I. N., Runswick, M. J., Walker, J. E. & Rubinstein, J. L. Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM. Proc. Natl Acad. Sci. USA 109, 11675-11680 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 11675-11680
    • Baker, L.A.1    Watt, I.N.2    Runswick, M.J.3    Walker, J.E.4    Rubinstein, J.L.5
  • 90
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • Eswar, N. et al. Comparative protein structure modeling using Modeller. Curr. Protoc. Bioinformatics 15, 5.6.1-5.6.30 (2006).
    • (2006) Curr. Protoc. Bioinformatics , vol.15 , pp. 561-563
    • Eswar, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.