메뉴 건너뛰기
Biochemistry (Moscow)
Volumn 76, Issue 2, 2011, Pages 209-216
Submitochondrial fragments of brain mitochondria: General characteristics and catalytic properties of NADH: Ubiquinone oxidoreductase (Complex I)
Author keywords

brain; complex I; mitochondria; NADH:ubiquinone oxidoreductase
Indexed keywords

BOVINAE;
EID: 79953881920     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297911020076     Document Type: Article
Times cited : (7)
References (59)
  • 1
    • 0027104114 scopus 로고
    • 10.1017/S003358350000425X 1:CAS:528:DyaK3sXps1KktQ%3D%3D
    • J. E. Walker 1992 Quart. Rev. Biophys. 25 253 324 10.1017/ S003358350000425X 1:CAS:528:DyaK3sXps1KktQ%3D%3D
    • (1992) Quart. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 4
    • 0027990677 scopus 로고
    • 8060976 10.1021/bi00199a034 1:CAS:528:DyaK2cXlt1ymsLo%3D
    • V. D. Sled N. I. Rudnitzky Y. Hatefi T. Ohnishi 1994 Biochemistry 33 10069 10075 8060976 10.1021/bi00199a034 1:CAS:528:DyaK2cXlt1ymsLo%3D
    • (1994) Biochemistry , vol.33 , pp. 10069-10075
    • Sled, V.D.1    Rudnitzky, N.I.2    Hatefi, Y.3    Ohnishi, T.4
  • 7
    • 0024435190 scopus 로고
    • Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain
    • DOI 10.1016/0014-5793(89)81007-5
    • D. Sh. Burbaev I. A. Moroz A. B. Kotlyar V. D. Sled A. D. Vinogradov 1989 FEBS Lett. 254 47 51 10.1016/0014-5793(89)81007-5 1:CAS:528:DyaL1MXlvFSit70%3D (Pubitemid 19217853)
    • (1989) FEBS Letters , vol.254 , Issue.1-2 , pp. 47-51
    • Burbaev, D.S.1    Moroz, I.A.2    Kotlyar, A.B.3    Sled, V.D.4    Vinogradov, A.D.5
  • 9
    • 0032311426 scopus 로고    scopus 로고
    • Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain
    • DOI 10.1016/S0005-2728(98)00082-6, PII S0005272898000826
    • T. Ohnishi V. D. Sled T. Yano T. Yagi D. S. Burbaev A. D. Vinogradov 1998 Biochim. Biophys. Acta 1365 301 308 9693742 10.1016/S0005-2728(98)00082-6 1:CAS:528:DyaK1cXksFKitLg%3D (Pubitemid 29359272)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1365 , Issue.1-2 , pp. 301-308
    • Ohnishi, T.1    Sled, V.D.2    Yano, T.3    Yagi, T.4    Burbaev, D.S.5    Vinogradov, A.D.6
  • 11
    • 36549055601 scopus 로고    scopus 로고
    • EXAFS reveals a structural zinc binding site in the bovine NADH-Q oxidoreductase
    • DOI 10.1016/j.febslet.2007.11.019, PII S0014579307011635
    • L. Giachini F. Francia F. Boscherini C. Pacelli T. Cocco S. Papa G. Venturoli 2007 FEBS Lett. 581 5645 5648 18022397 10.1016/j.febslet.2007.11.019 1:CAS:528:DC%2BD2sXhtlykt7rP (Pubitemid 350179774)
    • (2007) FEBS Letters , vol.581 , Issue.29 , pp. 5645-5648
    • Giachini, L.1    Francia, F.2    Boscherini, F.3    Pacelli, C.4    Cocco, T.5    Papa, S.6    Venturoli, G.7
  • 13
    • 0032490117 scopus 로고    scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • DOI 10.1016/S0005-2728(98)00024-3, PII S0005272898000243
    • T. Friedrich 1998 Biochim. Biophys. Acta 1364 134 146 9593861 10.1016/S0005-2728(98)00024-3 1:CAS:528:DyaK1cXis1Clsb8%3D (Pubitemid 28291836)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1364 , Issue.2 , pp. 134-146
    • Friedrich, T.1
  • 15
    • 0027268344 scopus 로고
    • 8226715 10.1007/BF00762459 1:CAS:528:DyaK3sXmsVCisrY%3D
    • T. Yagi T. Yano A. Matsuno-Yagi 1993 J. Bioenerg. Biomembr. 25 339 345 8226715 10.1007/BF00762459 1:CAS:528:DyaK3sXmsVCisrY%3D
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 339-345
    • Yagi, T.1    Yano, T.2    Matsuno-Yagi, A.3
  • 16
    • 23044477952 scopus 로고    scopus 로고
    • Biochemistry: Organization of iron-sulfur clusters in respiratory complex I
    • DOI 10.1126/science.1113988
    • P. Hinchliffe L. A. Sazanov 2005 Science 309 771 774 16051796 10.1126/science.1113988 1:CAS:528:DC%2BD2MXmsFWmsLw%3D (Pubitemid 41077323)
    • (2005) Science , vol.309 , Issue.5735 , pp. 771-774
    • Hinchliffe, P.1    Sazanov, L.A.2
  • 18
    • 0032490104 scopus 로고    scopus 로고
    • Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) and the pseudo-reversible active/inactive enzyme transition
    • DOI 10.1016/S0005-2728(98)00026-7, PII S0005272898000267
    • A. Vinogradov 1998 Biochim. Biophys. Acta 1364 169 185 9593879 10.1016/S0005-2728(98)00026-7 1:CAS:528:DyaK1cXis1Clsbs%3D (Pubitemid 28291838)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1364 , Issue.2 , pp. 169-185
    • Vinogradov, A.D.1
  • 19
    • 0035549868 scopus 로고    scopus 로고
    • Respiratory Complex I: Structure, redox components, and possible mechanisms of energy transduction
    • DOI 10.1023/A:1012476728710
    • A. D. Vinogradov 2001 Biochemistry (Moscow) 66 1086 1097 10.1023/A:1012476728710 1:CAS:528:DC%2BD3MXos1akurg%3D (Pubitemid 33099911)
    • (2001) Biochemistry (Moscow) , vol.66 , Issue.10 , pp. 1086-1097
    • Vinogradov, A.D.1
  • 20
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • DOI 10.1126/science.1123809
    • L. Sazanov P. Hinchliffe 2006 Science 311 1430 1436 16469879 10.1126/science.1123809 1:CAS:528:DC%2BD28XitVyjsbg%3D (Pubitemid 43376691)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 21
    • 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
    • L. A. Sazanov 2007 Biochemistry 46 2275 2288 17274631 10.1021/bi602508x 1:CAS:528:DC%2BD2sXht1ykt7g%3D (Pubitemid 46362402)
    • (2007) Biochemistry , vol.46 , Issue.9 , pp. 2275-2288
    • Sazanov, L.A.1
  • 22
    • 77952979824 scopus 로고    scopus 로고
    • 20505720 10.1038/nature09066 1:CAS:528:DC%2BC3cXmsF2itbc%3D
    • R. G. Efremov R. Baradaran L. Sazanov 2010 Nature 465 441 445 20505720 10.1038/nature09066 1:CAS:528:DC%2BC3cXmsF2itbc%3D
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.3
  • 23
    • 77954848120 scopus 로고    scopus 로고
    • 20595580 10.1126/science.1191046 1:CAS:528:DC%2BC3cXptVWgtrY%3D
    • C. Hunte V. Zickermann U. Brandt 2010 Science 329 448 451 20595580 10.1126/science.1191046 1:CAS:528:DC%2BC3cXptVWgtrY%3D
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 24
    • 0021769852 scopus 로고
    • 6325245 10.1016/0014-5793(84)80338-5 1:STN:280:DyaL2c7otlSnsA%3D%3D
    • M. Wikstrom 1984 FEBS Lett. 169 300 304 6325245 10.1016/0014-5793(84) 80338-5 1:STN:280:DyaL2c7otlSnsA%3D%3D
    • (1984) FEBS Lett. , vol.169 , pp. 300-304
    • Wikstrom, M.1
  • 25
    • 0032588194 scopus 로고    scopus 로고
    • +/2ē stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles
    • DOI 10.1016/S0014-5793(99)00575-X, PII S001457939900575X
    • A. S. Galkin V. G. Grivennikova A. D. Vinogradov 1999 FEBS Lett. 451 157 161 10371157 10.1016/S0014-5793(99)00575-X 1:CAS:528:DyaK1MXjsVSjtbw%3D (Pubitemid 29231941)
    • (1999) FEBS Letters , vol.451 , Issue.2 , pp. 157-161
    • Galkin, A.S.1    Grivennikova, V.G.2    Vinogradov, A.D.3
  • 29
    • 38049136885 scopus 로고    scopus 로고
    • 17956863 10.1074/jbc.M707543200 1:CAS:528:DC%2BD2sXhsVGjtrrI
    • A. Galkin S. Moncada 2007 J. Biol. Chem. 282 37448 37453 17956863 10.1074/jbc.M707543200 1:CAS:528:DC%2BD2sXhsVGjtrrI
    • (2007) J. Biol. Chem. , vol.282 , pp. 37448-37453
    • Galkin, A.1    Moncada, S.2
  • 32
    • 0032490114 scopus 로고    scopus 로고
    • Inhibitors of NADH-ubiquinone reductase: An overview
    • DOI 10.1016/S0005-2728(98)00029-2, PII S0005272898000292
    • M. Degli Esposti 1998 Biochim. Biophys. Acta 1364 222 235 9593904 10.1016/S0005-2728(98)00029-2 1:CAS:528:DyaK1cXis1Cltr4%3D (Pubitemid 28291841)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1364 , Issue.2 , pp. 222-235
    • Degli Esposti, M.1
  • 34
    • 0025072729 scopus 로고
    • Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase
    • DOI 10.1016/0005-2728(90)90137-S
    • A. B. Kotlyar A. D. Vinogradov 1990 Biochim. Biophys. Acta 1019 151 158 2119805 10.1016/0005-2728(90)90137-S 1:CAS:528:DyaK3MXhtlyls7Y%3D (Pubitemid 20257657)
    • (1990) Biochimica et Biophysica Acta - Bioenergetics , vol.1019 , Issue.2 , pp. 151-158
    • Kotlyar, A.B.1    Vinogradov, A.D.2
  • 35
    • 0021766207 scopus 로고
    • 6691982 10.1016/0167-4838(84)90168-7 1:CAS:528:DyaL2cXhtFOjs7k%3D
    • A. B. Kotlyar A. D. Vinogradov 1984 Biochim. Biophys. Acta 784 24 34 6691982 10.1016/0167-4838(84)90168-7 1:CAS:528:DyaL2cXhtFOjs7k%3D
    • (1984) Biochim. Biophys. Acta , vol.784 , pp. 24-34
    • Kotlyar, A.B.1    Vinogradov, A.D.2
  • 36
    • 0006387704 scopus 로고
    • J. M. Tager S. Papa E. Quagliariello E. C. Slater (eds). Elsevier Amsterdam
    • Lee, C. P., and Ernster, L. (1966) in BBA Library, Vol. 7 (Tager, J. M., Papa, S., Quagliariello, E., and Slater, E. C., eds.) Elsevier, Amsterdam, pp. 218-223.
    • (1966) BBA Library, Vol. 7 , pp. 218-223
    • Lee, C.P.1    Ernster, L.2
  • 37
    • 0014490869 scopus 로고
    • 4305534 10.1111/j.1432-1033.1969.tb00509.x 1:CAS:528:DyaF1MXosValtg%3D%3D
    • C. P. Lee L. Ernster B. Chance 1969 Eur. J. Biochem. 8 153 163 4305534 10.1111/j.1432-1033.1969.tb00509.x 1:CAS:528:DyaF1MXosValtg%3D%3D
    • (1969) Eur. J. Biochem. , vol.8 , pp. 153-163
    • Lee, C.P.1    Ernster, L.2    Chance, B.3
  • 39
  • 41
    • 77049249588 scopus 로고
    • 13271404 1:CAS:528:DyaG28XitVGhtg%3D%3D
    • B. Chance G. Williams 1955 J. Biol. Chem. 217 409 428 13271404 1:CAS:528:DyaG28XitVGhtg%3D%3D
    • (1955) J. Biol. Chem. , vol.217 , pp. 409-428
    • Chance, B.1    Williams, G.2
  • 42
    • 0018337780 scopus 로고
    • 156830 10.1016/0076-6879(79)55017-4 1:CAS:528:DyaE1MXmtVKrsLw%3D
    • A. Vinogradov T. E. King 1979 Meth. Enzymol. 55 118 127 156830 10.1016/0076-6879(79)55017-4 1:CAS:528:DyaE1MXmtVKrsLw%3D
    • (1979) Meth. Enzymol. , vol.55 , pp. 118-127
    • Vinogradov, A.1    King, T.E.2
  • 43
    • 0037328645 scopus 로고    scopus 로고
    • In situ assay of the intramitochondrial enzymes: Use of alamethicin for permeabilization of mitochondria
    • DOI 10.1016/S0003-2697(02)00534-1, PII S0003269702005341
    • I. S. Gostimskaya V. G. Grivennikova T. V. Zharova L. E. Bakeeva A. D. Vinogradov 2003 Anal. Biochem. 313 46 52 12576057 10.1016/S0003-2697(02)00534-1 1:CAS:528:DC%2BD3sXotlOqtA%3D%3D (Pubitemid 36268816)
    • (2003) Analytical Biochemistry , vol.313 , Issue.1 , pp. 46-52
    • Gostimskaya, I.S.1    Grivennikova, V.G.2    Zharova, T.V.3    Bakeeva, L.E.4    Vinogradov, A.D.5
  • 45
    • 33745628757 scopus 로고    scopus 로고
    • Generation of superoxide by the mitochondrial Complex I
    • DOI 10.1016/j.bbabio.2006.03.013, PII S0005272806000685
    • V. Grivennikova A. Vinogradov 2006 Biochim. Biophys. Acta 1757 553 561 16678117 10.1016/j.bbabio.2006.03.013 1:CAS:528:DC%2BD28Xmsl2jt7o%3D (Pubitemid 43993849)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.5-6 , pp. 553-561
    • Grivennikova, V.G.1    Vinogradov, A.D.2
  • 46
    • 24044544620 scopus 로고    scopus 로고
    • A novel strong competitive inhibitor of complex I
    • DOI 10.1016/j.febslet.2005.07.076, PII S0014579305009440
    • A. Kotlyar J. S. Karliner G. Cecchini 2005 FEBS Lett. 579 4861 4866 16107251 10.1016/j.febslet.2005.07.076 1:CAS:528:DC%2BD2MXpt1eru7Y%3D (Pubitemid 41218676)
    • (2005) FEBS Letters , vol.579 , Issue.21 , pp. 4861-4866
    • Kotlyar, A.B.1    Karliner, J.S.2    Cecchini, G.3
  • 48
    • 0007715066 scopus 로고
    • 4378680 10.1038/206257a0 1:CAS:528:DyaF2MXktFWiurY%3D
    • B. Chance D. Jamieson H. Coles 1965 Nature 206 257 263 4378680 10.1038/206257a0 1:CAS:528:DyaF2MXktFWiurY%3D
    • (1965) Nature , vol.206 , pp. 257-263
    • Chance, B.1    Jamieson, D.2    Coles, H.3
  • 50
    • 0018164454 scopus 로고
    • 713832 10.1016/S0076-6879(78)53006-1 1:CAS:528:DyaE1MXkvVKjurs%3D
    • Y. Hatefi 1978 Meth. Enzymol. 53 11 14 713832 10.1016/S0076-6879(78) 53006-1 1:CAS:528:DyaE1MXkvVKjurs%3D
    • (1978) Meth. Enzymol. , vol.53 , pp. 11-14
    • Hatefi, Y.1
  • 51
    • 30144445462 scopus 로고    scopus 로고
    • Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondrial
    • DOI 10.1021/bi051809x
    • M. S. Sharpley R. J. Shannon F. Draghi J. Hirst 2006 Biochemistry 45 241 248 16388600 10.1021/bi051809x 1:CAS:528:DC%2BD2MXht12jsb%2FF (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
  • 54
    • 0036139815 scopus 로고    scopus 로고
    • 11798024 10.1080/15216540152845920 1:CAS:528:DC%2BD38Xlt1Wmuw%3D%3D
    • A. Vinogradov V. Grivennikova 2001 IUBMB Life 52 129 134 11798024 10.1080/15216540152845920 1:CAS:528:DC%2BD38Xlt1Wmuw%3D%3D
    • (2001) IUBMB Life , vol.52 , pp. 129-134
    • Vinogradov, A.1    Grivennikova, V.2
  • 55
    • 0037325411 scopus 로고    scopus 로고
    • The transition between active and de-activated forms of NADH: Ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa
    • DOI 10.1042/BJ20021165
    • V. Grivennikova D. Serebryanaya E. Isakova T. Belozerskaya A. Vinogradov 2003 Biochem. J. 369 619 626 12379145 10.1042/BJ20021165 1:CAS:528: DC%2BD3sXit1aqu7Y%3D (Pubitemid 36246245)
    • (2003) Biochemical Journal , vol.369 , Issue.3 , pp. 619-626
    • Grivennikova, V.G.1    Serebryanaya, D.V.2    Isakova, E.P.3    Belozerskaya, T.A.4    Vinogradov, A.D.5
  • 56
    • 0142106477 scopus 로고    scopus 로고
    • Active/de-active transition of respiratory complex I in bacteria, fungi, and animals
    • DOI 10.1016/S0005-2728(03)00087-2
    • E. Maklashina A. Kotlyar G. Cecchini 2003 Biochim. Biophys. Acta 1606 95 103 14507430 10.1016/S0005-2728(03)00087-2 1:CAS:528:DC%2BD3sXnsVagur8%3D (Pubitemid 37267873)
    • (2003) Biochimica et Biophysica Acta - Bioenergetics , vol.1606 , Issue.1-3 , pp. 95-103
    • Maklashina, E.1    Kotlyar, A.B.2    Cecchini, G.3
  • 59
    • 33748975921 scopus 로고    scopus 로고
    • Topography and chemical reactivity of the active-inactive transition-sensitive SH-group in the mitochondrial NADH:ubiquinone oxidoreductase (Complex I)
    • DOI 10.1016/j.bbabio.2006.04.016, PII S0005272806001125, Mitochondria: from Molecular Insight to Physiology and Pathology
    • I. S. Gostimskaya G. Cecchini A. D. Vinogradov 2006 Biochim. Biophys. Acta 1757 1155 1161 16777054 10.1016/j.bbabio.2006.04.016 1:CAS:528: DC%2BD28XhtVanurjF (Pubitemid 44442115)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.9-10 , pp. 1155-1161
    • Gostimskaya, I.S.1    Cecchini, G.2    Vinogradov, A.D.3

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.