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Volumn 51, Issue 9, 2012, Pages 1953-1963

Fenpyroximate binds to the interface between PSST and 49 kDa subunits in mitochondrial NADH-Ubiquinone oxidoreductase

Author keywords

[No Author keywords available]

Indexed keywords

AZIDO GROUP; BOVINE HEART; CORE MOIETY; CRITICAL QUESTIONS; FRAGMENTATION PATTERNS; LIMITED PROTEOLYSIS; MEMBRANE DOMAIN; OXIDOREDUCTASES; PHOTOAFFINITY LABELING; PYRAZOLE RING; SIDE-CHAINS; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; TRANSMEMBRANE HELIX; TWO DOMAINS;

EID: 84857872726     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300047h     Document Type: Article
Times cited : (49)

References (47)
  • 1
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • Brandt, U. (2006) Energy converting NADH:quinone oxidoreductase (complex I) Annu. Rev. Biochem. 75, 69-92
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 69-92
    • Brandt, U.1
  • 2
    • 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
  • 4
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex i from Thermus thermophilus
    • Sazanov, L. A. and Hinchliffe, P. (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus Science 311, 1430-1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 5
    • 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
  • 6
    • 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
  • 10
    • 0347295939 scopus 로고    scopus 로고
    • The ND5 subunit was labeled by a photoaffinity analogue of fenpyroximate in bovine mitochondrial complex i
    • Nakamaru-Ogiso, E., Sakamoto, K., Matsuno-Yagi, A., Miyoshi, H., and Yagi, T. (2003) The ND5 subunit was labeled by a photoaffinity analogue of fenpyroximate in bovine mitochondrial complex I Biochemistry 42, 746-754
    • (2003) Biochemistry , vol.42 , pp. 746-754
    • Nakamaru-Ogiso, E.1    Sakamoto, K.2    Matsuno-Yagi, A.3    Miyoshi, H.4    Yagi, T.5
  • 11
    • 34249684873 scopus 로고    scopus 로고
    • The ND1 subunit constructs the inhibitor binding domain in bovine heart mitochondrial complex i
    • Murai, M., Ishihara, A., Nishioka, T., Yagi, T., and Miyoshi, H. (2007) The ND1 subunit constructs the inhibitor binding domain in bovine heart mitochondrial complex I Biochemistry 46, 6409-6416
    • (2007) Biochemistry , vol.46 , pp. 6409-6416
    • Murai, M.1    Ishihara, A.2    Nishioka, T.3    Yagi, T.4    Miyoshi, H.5
  • 12
    • 53249107720 scopus 로고    scopus 로고
    • Synthesis and characterization of new piperazine-type inhibitors for mitochondrial NADH-ubiquinone oxidoreductase (complex I)
    • Ichimaru, N., Murai, M., Kakutani, N., Kako, J., Ishihara, A., Nakagawa, Y., Nishioka, T., Yagi, T., and Miyoshi, H. (2008) Synthesis and characterization of new piperazine-type inhibitors for mitochondrial NADH-ubiquinone oxidoreductase (complex I) Biochemistry 47, 10816-10826
    • (2008) Biochemistry , vol.47 , pp. 10816-10826
    • Ichimaru, N.1    Murai, M.2    Kakutani, N.3    Kako, J.4    Ishihara, A.5    Nakagawa, Y.6    Nishioka, T.7    Yagi, T.8    Miyoshi, H.9
  • 13
    • 60749121178 scopus 로고    scopus 로고
    • Characterization of the inhibitor binding site in mitochondrial NADH-ubiquinone oxidoreductase by photoaffinity labeling using a quinazoline-type inhibitor
    • Murai, M., Sekiguchi, K., Nishioka, T., and Miyoshi, H. (2009) Characterization of the inhibitor binding site in mitochondrial NADH-ubiquinone oxidoreductase by photoaffinity labeling using a quinazoline-type inhibitor Biochemistry 48, 688-698
    • (2009) Biochemistry , vol.48 , pp. 688-698
    • Murai, M.1    Sekiguchi, K.2    Nishioka, T.3    Miyoshi, H.4
  • 14
    • 77953279656 scopus 로고    scopus 로고
    • Exploring the binding site of Δlac-acetogenin in bovine heart mitochondrial NADH-ubiquinone oxidoreductase
    • Kakutani, N., Murai, M., Sakiyama, N., and Miyoshi, H. (2010) Exploring the binding site of Δlac-acetogenin in bovine heart mitochondrial NADH-ubiquinone oxidoreductase Biochemistry 49, 4794-4803
    • (2010) Biochemistry , vol.49 , pp. 4794-4803
    • Kakutani, N.1    Murai, M.2    Sakiyama, N.3    Miyoshi, H.4
  • 15
    • 80051499873 scopus 로고    scopus 로고
    • Exploring interactions between the 49 kDa and ND1 subunits in mitochondrial NADH-ubiquinone oxidoreductase (complex I) by photoaffinity labeling
    • Murai, M., Mashimo, Y., Hirst, J., and Miyoshi, H. (2011) Exploring interactions between the 49 kDa and ND1 subunits in mitochondrial NADH-ubiquinone oxidoreductase (complex I) by photoaffinity labeling Biochemistry 50, 6901-6908
    • (2011) Biochemistry , vol.50 , pp. 6901-6908
    • Murai, M.1    Mashimo, Y.2    Hirst, J.3    Miyoshi, H.4
  • 16
    • 35748979985 scopus 로고    scopus 로고
    • Exploring the ubiquinone binding cavity of respiratory complex i
    • Tocilescu, M. A., Fendel, U., Zwicker, K., Kerscher, S., and Brandt, U. (2007) Exploring the ubiquinone binding cavity of respiratory complex I J. Biol. Chem. 282, 29514-29520
    • (2007) J. Biol. Chem. , vol.282 , pp. 29514-29520
    • Tocilescu, M.A.1    Fendel, U.2    Zwicker, K.3    Kerscher, S.4    Brandt, U.5
  • 17
    • 50949091505 scopus 로고    scopus 로고
    • Exploring the inhibitor binding pocket of respiratory complex i
    • Fendel, U., Tocilescu, M. A., Kerscher, S., and Brandt, U. (2008) Exploring the inhibitor binding pocket of respiratory complex I Biochim. Biophys. Acta 1777, 660-665
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 660-665
    • Fendel, U.1    Tocilescu, M.A.2    Kerscher, S.3    Brandt, U.4
  • 18
    • 0344820721 scopus 로고    scopus 로고
    • Three classes of inhibitor share a common binding domain in mitochondrial complex i (NADH-ubiquinone oxidoreductase)
    • Okun, J. G., Lümmen, P., and Brandt, U. (1999) Three classes of inhibitor share a common binding domain in mitochondrial complex I (NADH-ubiquinone oxidoreductase) J. Biol. Chem. 274, 2625-2630
    • (1999) J. Biol. Chem. , vol.274 , pp. 2625-2630
    • Okun, J.G.1    Lümmen, P.2    Brandt, U.3
  • 19
    • 76749117977 scopus 로고    scopus 로고
    • The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex i inhibitor
    • Nakamaru-Ogiso, E., Han, H., Matsuno-Yagi, A., Keinan, E., Sinha, S. C., Yagi, T., and Ohnishi, T. (2010) The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor FEBS Lett. 584, 883-888
    • (2010) FEBS Lett. , vol.584 , pp. 883-888
    • Nakamaru-Ogiso, E.1    Han, H.2    Matsuno-Yagi, A.3    Keinan, E.4    Sinha, S.C.5    Yagi, T.6    Ohnishi, T.7
  • 20
    • 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., Kao, M.-C., Chen, H., Sinha, S. C., Yagi, T., and Ohnishi, T. (2010) 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) J. Biol. Chem. , vol.285 , pp. 39070-39078
    • Nakamaru-Ogiso, E.1    Kao, M.-C.2    Chen, H.3    Sinha, S.C.4    Yagi, T.5    Ohnishi, T.6
  • 21
    • 79957477189 scopus 로고    scopus 로고
    • Decoupling of catalytic transport activities of Rhodothermus marinus complex i by a sodium/proton antiporter inhibitor
    • Batista, A. P., Marreiros, B. C., and Pereira, M. M. (2011) Decoupling of catalytic transport activities of Rhodothermus marinus complex I by a sodium/proton antiporter inhibitor ACS Chem. Biol. 6, 477-483
    • (2011) ACS Chem. Biol. , vol.6 , pp. 477-483
    • Batista, A.P.1    Marreiros, B.C.2    Pereira, M.M.3
  • 22
    • 79751524661 scopus 로고    scopus 로고
    • Homologous protein subunits from Escherichia coli NADH-quinonone oxidoreductase can functionally replace MrpA and MrpD in Bacillus subtilis
    • Moparthi, V. K., Kumar, B., Mathiesen, C., and Hägerhäll, C. (2011) Homologous protein subunits from Escherichia coli NADH-quinonone oxidoreductase can functionally replace MrpA and MrpD in Bacillus subtilis Biochim. Biophys. Acta 1807, 427-436
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 427-436
    • Moparthi, V.K.1    Kumar, B.2    Mathiesen, C.3    Hägerhäll, C.4
  • 23
    • 79952236392 scopus 로고    scopus 로고
    • Mutagenesis of the L, M, and N subunits of complex i from Escherichia coli indicates a common role in function
    • Michel, J., Deleon-Rangel, J., Zhu, S., Van Ree, K., and Vik, S. B. (2011) Mutagenesis of the L, M, and N subunits of complex I from Escherichia coli indicates a common role in function PLoS One 6, e17420
    • (2011) PLoS One , vol.6 , pp. 17420
    • Michel, J.1    Deleon-Rangel, J.2    Zhu, S.3    Van Ree, K.4    Vik, S.B.5
  • 24
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex i
    • Efremov, R. G. and Sazanov, L. A. (2011) Structure of the membrane domain of respiratory complex I Nature 476, 414-420
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 25
    • 0022400789 scopus 로고
    • Studies on the mechanism of oxidative phosphorylation
    • Matsuno-Yagi, A. and Hatefi, Y. (1985) Studies on the mechanism of oxidative phosphorylation J. Biol. Chem. 260, 14424-14427
    • (1985) J. Biol. Chem. , vol.260 , pp. 14424-14427
    • Matsuno-Yagi, A.1    Hatefi, Y.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger, H. (2006) Tricine-SDS-PAGE Nat. Protoc. 1, 16-21
    • (2006) Nat. Protoc. , vol.1 , pp. 16-21
    • Schägger, H.1
  • 28
    • 3543043510 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification
    • Rais, I., Kara, M., and Schägger, H. (2004) Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification Proteomics 4, 2567-2571
    • (2004) Proteomics , vol.4 , pp. 2567-2571
    • Rais, I.1    Kara, M.2    Schägger, H.3
  • 29
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland, D. W., Fishcher, M. W., Kirschner, M. W., and Laemmli, U. K. (1977) Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis J. Biol. Chem. 252, 1102-1106
    • (1977) J. Biol. Chem. , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fishcher, M.W.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 31
    • 21844515139 scopus 로고
    • Development of acaricide fenpyroximate
    • Hamaguchi, H., Kajihara, O., and Katoh, M. (1995) Development of acaricide fenpyroximate J. Pestic. Sci. 20, 203-212
    • (1995) J. Pestic. Sci. , vol.20 , pp. 203-212
    • Hamaguchi, H.1    Kajihara, O.2    Katoh, M.3
  • 32
    • 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., Meyer, B., Wittig, I., Karas, M., Schägger, H., Vinogradov, A., and Brandt, U. (2008) 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) J. Biol. Chem. , vol.283 , pp. 20907-20913
    • Galkin, A.1    Meyer, B.2    Wittig, I.3    Karas, M.4    Schägger, H.5    Vinogradov, A.6    Brandt, U.7
  • 35
    • 67649494451 scopus 로고    scopus 로고
    • Exploring the binding site of acetogenin in the ND1 subunit of bovine mitochondrial complex i
    • Sekiguchi, K., Murai, M., and Miyoshi, H. (2009) Exploring the binding site of acetogenin in the ND1 subunit of bovine mitochondrial complex I Biochim. Biophys. Acta 1787, 1106-1111
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1106-1111
    • Sekiguchi, K.1    Murai, M.2    Miyoshi, H.3
  • 36
    • 79960558556 scopus 로고    scopus 로고
    • Bis-THF motif of acetogenin binds to the third matrix-side loop of ND1 subunit in mitochondrial NADH-ubiquinone oxidoreductase
    • Nakanishi, S., Abe, M., Yamamoto, S., Murai, M., and Miyoshi, H. (2011) Bis-THF motif of acetogenin binds to the third matrix-side loop of ND1 subunit in mitochondrial NADH-ubiquinone oxidoreductase Biochim. Biophys. Acta 1807, 1170-1176
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1170-1176
    • Nakanishi, S.1    Abe, M.2    Yamamoto, S.3    Murai, M.4    Miyoshi, H.5
  • 37
    • 1642392110 scopus 로고    scopus 로고
    • +-translocating NADH-quinone oxidoreductase probed by zero-length cross-linking
    • +-translocating NADH-quinone oxidoreductase probed by zero-length cross-linking Biochemistry 43, 3750-3755
    • (2004) Biochemistry , vol.43 , pp. 3750-3755
    • Kao, M.-C.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 38
    • 77957128550 scopus 로고    scopus 로고
    • Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter-like subunits in complex i from higher metazoans
    • Birrell, J. A. and Hirst, J. (2010) Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter-like subunits in complex I from higher metazoans FEBS Lett. 584, 4247-4252
    • (2010) FEBS Lett. , vol.584 , pp. 4247-4252
    • Birrell, J.A.1    Hirst, J.2
  • 39
  • 41
    • 0037815067 scopus 로고    scopus 로고
    • The ubiquinone-binding site in NADH-ubiquinone oxidoreductase from Escherichia coli
    • Gong, X., Xie, T., Yu, L., Hesterberg, M., Scheide, D., Friedrich, T., and Yu, C.-A. (2003) The ubiquinone-binding site in NADH-ubiquinone oxidoreductase from Escherichia coli J. Biol. Chem. 278, 25731-25737
    • (2003) J. Biol. Chem. , vol.278 , pp. 25731-25737
    • Gong, X.1    Xie, T.2    Yu, L.3    Hesterberg, M.4    Scheide, D.5    Friedrich, T.6    Yu, C.-A.7
  • 42
    • 33644848768 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli
    • Matsumoto, Y., Murai, M., Fujita, D., Sakamoto, K., Miyoshi, H., Yoshida, M., and Mogi, T. (2006) Mass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli J. Biol. Chem. 281, 1905-1912
    • (2006) J. Biol. Chem. , vol.281 , pp. 1905-1912
    • Matsumoto, Y.1    Murai, M.2    Fujita, D.3    Sakamoto, K.4    Miyoshi, H.5    Yoshida, M.6    Mogi, T.7
  • 43
    • 37549049790 scopus 로고    scopus 로고
    • Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: Conserved charged residues essential for energy-coupled activities
    • Torres-Bacete, J., Nakamaru-Ogiso, E., Matsuno-Yagi, A., and Yagi, T. (2007) Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: Conserved charged residues essential for energy-coupled activities J. Biol. Chem. 282, 36914-36922
    • (2007) J. Biol. Chem. , vol.282 , pp. 36914-36922
    • Torres-Bacete, J.1    Nakamaru-Ogiso, E.2    Matsuno-Yagi, A.3    Yagi, T.4
  • 44
    • 0037136017 scopus 로고    scopus 로고
    • Essential structural factors of acetogenins, potent inhibitors of mitochondrial complex i
    • Motoyama, T., Yabunaka, H., and Miyoshi, H. (2002) Essential structural factors of acetogenins, potent inhibitors of mitochondrial complex I Bioorg. Med. Chem. Lett. 12, 2089-2092
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 2089-2092
    • Motoyama, T.1    Yabunaka, H.2    Miyoshi, H.3
  • 45
    • 27744541418 scopus 로고    scopus 로고
    • Dynamic function of the alkyl spacer of acetogenins in their inhibitory action with mitochondrial complex i (NADH-ubiquinone oxidoreductase)
    • Abe, M., Murai, M., Ichimaru, N., Kenmochi, A., Yoshida, T., Kubo, A., Kimura, Y., Moroda, A., Makabe, H., Nishioka, T., and Miyoshi, H. (2005) Dynamic function of the alkyl spacer of acetogenins in their inhibitory action with mitochondrial complex I (NADH-ubiquinone oxidoreductase) Biochemistry 44, 14898-14906
    • (2005) Biochemistry , vol.44 , pp. 14898-14906
    • Abe, M.1    Murai, M.2    Ichimaru, N.3    Kenmochi, A.4    Yoshida, T.5    Kubo, A.6    Kimura, Y.7    Moroda, A.8    Makabe, H.9    Nishioka, T.10    Miyoshi, H.11
  • 46
    • 44949164731 scopus 로고    scopus 로고
    • Dynamic function of the spacer region of acetogenins in the inhibition of bovine mitochondrial NADH-ubiquinone oxidoreductase (complex I)
    • Abe, M., Kubo, A., Yamamoto, S., Hatoh, Y., Murai, M., Hattori, Y., Makabe, H., Nishioka, T., and Miyoshi, H. (2008) Dynamic function of the spacer region of acetogenins in the inhibition of bovine mitochondrial NADH-ubiquinone oxidoreductase (complex I) Biochemistry 47, 6260-6266
    • (2008) Biochemistry , vol.47 , pp. 6260-6266
    • Abe, M.1    Kubo, A.2    Yamamoto, S.3    Hatoh, Y.4    Murai, M.5    Hattori, Y.6    Makabe, H.7    Nishioka, T.8    Miyoshi, H.9
  • 47
    • 80051601805 scopus 로고    scopus 로고
    • A two-state stabilization-change mechanism for proton-pumping complex i
    • Brandt, U. (2011) A two-state stabilization-change mechanism for proton-pumping complex I Biochim. Biophys. Acta 1807, 1364-1369
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1364-1369
    • Brandt, U.1


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