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Volumn 109, Issue 9, 2012, Pages 3275-3280

Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors

Author keywords

Cyanide inhibition; Cytochrome c oxidase; Protein complex interaction; Quinol oxidase

Indexed keywords

ALCOHOL DERIVATIVE; CYTOCHROME C; CYTOCHROME C OXIDASE; DECYLUBIQUINOL; HEME COPPER TERMINAL OXIDASE; MULTIENZYME COMPLEX; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SULFIDE QUINONE OXIDOREDUCTASE; UBIQUINOL; UBIQUINOL CYTOCHROME C REDUCTASE; UBIQUINONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84863277606     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1121040109     Document Type: Article
Times cited : (24)

References (41)
  • 1
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • Saraste M (1999) Oxidative phosphorylation at the fin de siecle. Science 283:1488-1493.
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 2
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thony-Meyer L (1997) Biogenesis of respiratory cytochromes in bacteria. Microbiol Mol Biol Rev 61:337-376.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 337-376
    • Thony-Meyer, L.1
  • 3
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • DOI 10.1016/S0005-2728(01)00169-4, PII S0005272801001694
    • Pereira MM, Santana M, Teixeira M (2001) A novel scenario for the evolution of haem-copper oxygen reductases. Biochim Biophys Acta 1505:185-208. (Pubitemid 32378771)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1505 , Issue.2-3 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 4
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H (1995) Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 6
    • 0033788953 scopus 로고    scopus 로고
    • The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site
    • Abramson J, et al. (2000) The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat Struct Biol 7:910-917.
    • (2000) Nat Struct Biol , vol.7 , pp. 910-917
    • Abramson, J.1
  • 7
    • 0021918980 scopus 로고
    • 3 complexes
    • Berry EA, Trumpower BL (1985) Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochrome c-aa3 complexes. J Biol Chem 260:2458-2467. (Pubitemid 15104854)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.4 , pp. 2458-2467
    • Berry, E.A.1    Trumpower, B.L.2
  • 8
    • 33745943572 scopus 로고    scopus 로고
    • Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes
    • Krause F (2006) Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes. Electrophoresis 27:2759-2781.
    • (2006) Electrophoresis , vol.27 , pp. 2759-2781
    • Krause, F.1
  • 11
    • 35848929504 scopus 로고    scopus 로고
    • 1 from bovine heart mitochondria
    • DOI 10.1021/bi700983h
    • Schafer E, Dencher NA, Vonck J, Parcej DN (2007) Three-dimensional structure of the respiratory chain supercomplex I1III2IV1 from bovine heart mitochondria. Biochemistry 46:12579-12585. (Pubitemid 350060084)
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12579-12585
    • Schafer, E.1    Dencher, N.A.2    Vonck, J.3    Parcej, D.N.4
  • 12
    • 34249688217 scopus 로고    scopus 로고
    • A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria
    • DOI 10.1074/jbc.M610545200
    • Heinemeyer J, Braun HP, Boekema EJ, Kouril R (2007) A structural model of the cytochrome C reductase/oxidase supercomplex from yeast mitochondria. J Biol Chem 282:12240-12248. (Pubitemid 47100694)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 12240-12248
    • Heinemeyer, J.1    Braun, H.-P.2    Boekema, E.J.3    Kouril, R.4
  • 15
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P (1976) Possible molecular mechanisms of the protonmotive function of cytochrome systems. J Theor Biol 62:327-367.
    • (1976) J Theor Biol , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 18
    • 65249140547 scopus 로고    scopus 로고
    • New insights into the respiratory chains of the chemolithoautotrophic and hyperthermophilic bacterium Aquifex aeolicus
    • Guiral M, et al. (2009) New insights into the respiratory chains of the chemolithoautotrophic and hyperthermophilic bacterium Aquifex aeolicus. J Proteome Res 8:1717-1730.
    • (2009) J Proteome Res , vol.8 , pp. 1717-1730
    • Guiral, M.1
  • 19
    • 78650633208 scopus 로고    scopus 로고
    • New functional sulfide oxidase-oxygen reductase supercomplex in the membrane of the hyperthermophilic bacterium Aquifex aeolicus
    • Prunetti L, et al. (2010) New functional sulfide oxidase-oxygen reductase supercomplex in the membrane of the hyperthermophilic bacterium Aquifex aeolicus. J Biol Chem 285:41815-41826.
    • (2010) J Biol Chem , vol.285 , pp. 41815-41826
    • Prunetti, L.1
  • 20
    • 77956504730 scopus 로고    scopus 로고
    • Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide-quinone oxidoreductase
    • Marcia M, et al. (2010) Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide-quinone oxidoreductase. Biochim Biophys Acta 1798:2114-2123.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 2114-2123
    • Marcia, M.1
  • 21
    • 79959687305 scopus 로고    scopus 로고
    • The elusive third subunit IIa of the bacterial B-type oxidases: The enzyme from the hyperthermophile Aquifex aeolicus
    • Prunetti L, Brugna M, Lebrun R, Giudici-Orticoni MT, Guiral M (2011) The elusive third subunit IIa of the bacterial B-type oxidases: The enzyme from the hyperthermophile Aquifex aeolicus. PLoS One 6:e21616.
    • (2011) PLoS One , vol.6
    • Prunetti, L.1    Brugna, M.2    Lebrun, R.3    Giudici-Orticoni, M.T.4    Guiral, M.5
  • 23
    • 0031282998 scopus 로고    scopus 로고
    • 3from Natronobacterium pharaonis - An archaeal four-subunit cytochrome-c-type oxidase
    • 3 from Natronobacterium pharaonis - an archaeal four-subunit cytochrome-c-type oxidase. Eur J Biochem 250:332-341.
    • (1997) Eur J Biochem , vol.250 , pp. 332-341
    • Mattar, S.1    Engelhard, M.2
  • 24
    • 0031039161 scopus 로고    scopus 로고
    • The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization
    • Purschke WG, Schmidt CL, Petersen A, Schafer G (1997) The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization. J Bacteriol 179:1344-1353. (Pubitemid 27076601)
    • (1997) Journal of Bacteriology , vol.179 , Issue.4 , pp. 1344-1353
    • Purschke, W.G.1    Schmidt, C.L.2    Petersen, A.3    Schafer, G.4
  • 25
    • 0026563750 scopus 로고
    • An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes
    • Lubben M, Kolmerer B, Saraste M (1992) An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes. EMBO J 11:805-812.
    • (1992) EMBO J , vol.11 , pp. 805-812
    • Lubben, M.1    Kolmerer, B.2    Saraste, M.3
  • 28
    • 11944264512 scopus 로고
    • Reaction of cyanide with cytochrome ba3 from Thermus thermophilus: Spectroscopic characterization of the Fe(II)a3-CN.Cu(II)B-CN complex suggests four 14N atoms are coordinated to CuB
    • Surerus KK, et al. (1992) Reaction of cyanide with cytochrome ba3 from Thermus thermophilus: Spectroscopic characterization of the Fe(II)a3-CN.Cu(II)B- CN complex suggests four 14N atoms are coordinated to CuB. Proc Natl Acad Sci USA 89:3195-3199.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3195-3199
    • Surerus, K.K.1
  • 29
    • 0020479091 scopus 로고
    • Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c
    • Antalis TM, Palmer G (1982) Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c. J Biol Chem 257:6194-6206.
    • (1982) J Biol Chem , vol.257 , pp. 6194-6206
    • Antalis, T.M.1    Palmer, G.2
  • 30
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas PE, Ryan D, LevinW (1976) An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal Biochem 75:168-176.
    • (1976) Anal Biochem , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 31
    • 0017335537 scopus 로고
    • Heme spin states of cytochrome c oxidase derived from room temperature magnetic susceptibility measurements
    • DOI 10.1016/0014-5793(77)80044-6
    • Falk KE, Vanngard T, Angstrom J (1977) Heme spin-states of cytochrome c oxidase derived from room temperature magnetic susceptibility measurements. FEBS Lett 75:23-27. (Pubitemid 8080270)
    • (1977) FEBS Letters , vol.75 , Issue.1 , pp. 23-27
    • Falk, K.E.1    Vanngard, T.2    Angstrom, J.3
  • 32
    • 0017402628 scopus 로고
    • Variable temperature magnetic circular dichroism spectra of cytochrome c oxidase and its derivatives
    • Thomson AJ, Brittain T, Greenwood C, Springall JP (1977) Variable-temperature magnetic-circular-dichroism spectra of cytochrome c oxidase and its derivatives. Biochem J 165:327-336. (Pubitemid 8154793)
    • (1977) Biochemical Journal , vol.165 , Issue.2 , pp. 327-336
    • Thomson, A.J.1    Brittain, T.2    Greenwood, C.3    Springall, J.P.4
  • 33
    • 0018232599 scopus 로고
    • Electronic state of heme in cytochrome oxidase III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7-200 K. Direct evidence for an antiferromagnetically coupled Fe(III)/Cu(II) pair
    • Tweedle MF, Wilson LJ (1978) Electronic state of heme in cytochrome oxidase III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7-200 K. Direct evidence for an antiferromagnetically coupled Fe (III)/Cu (II) pair. J Biol Chem 253:8065-8071. (Pubitemid 9086286)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.22 , pp. 8065-8071
    • Tweedle, M.F.1    Wilson, L.J.2    Garcia-Iniguez, L.3
  • 35
    • 1942536490 scopus 로고    scopus 로고
    • Interaction of cytochrome c with cytochrome oxidase: Two different docking scenarios
    • DOI 10.1016/j.bbabio.2003.10.010, PII S0005272803002068
    • Maneg O, Malatesta F, Ludwig B, Drosou V (2004) Interaction of cytochrome c with cytochrome oxidase: Two different docking scenarios. Biochim Biophys Acta 1655:274-281. (Pubitemid 38526190)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1655 , Issue.1-3 , pp. 274-281
    • Maneg, O.1    Malatesta, F.2    Ludwig, B.3    Drosou, V.4
  • 36
    • 0027172336 scopus 로고
    • Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view
    • DOI 10.1016/0014-5793(93)80156-O
    • Musser SM, Stowell MH, Chan SI (1993) Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view. FEBS Lett 327:131-136. (Pubitemid 23211175)
    • (1993) FEBS Letters , vol.327 , Issue.2 , pp. 131-136
    • Musser, S.M.1    Stowell, M.H.B.2    Chan, S.I.3
  • 37
    • 0028137093 scopus 로고
    • The cytochrome oxidase superfamily of redox-driven proton pumps
    • DOI 10.1016/0968-0004(94)90071-X
    • Calhoun MW, Thomas JW, Gennis RB (1994) The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem Sci 19:325-330. (Pubitemid 24259984)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.8 , pp. 325-330
    • Calhoun, M.W.1    Thomas, J.W.2    Gennis, R.B.3
  • 38
    • 79960581689 scopus 로고    scopus 로고
    • Adaptation of aerobic respiration to low O2 environments
    • Han H, et al. (2011) Adaptation of aerobic respiration to low O2 environments. Proc Natl Acad Sci USA 108:14109-14114.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14109-14114
    • Han, H.1
  • 39
    • 0031688652 scopus 로고    scopus 로고
    • 3-type cytochrome c oxidase from Thermus thermophilus
    • DOI 10.1016/S0014-5793(98)00942-9, PII S0014579398009429
    • Kannt A, et al. (1998) Electrical current generation and proton pumping catalyzed by the ba3-type cytochrome c oxidase from Thermus thermophilus. FEBS Lett 434:17-22. (Pubitemid 28404654)
    • (1998) FEBS Letters , vol.434 , Issue.1-2 , pp. 17-22
    • Kannt, A.1    Soulimane, T.2    Buse, G.3    Becker, A.4    Bamberg, E.5    Michel, H.6
  • 40
    • 67649872642 scopus 로고    scopus 로고
    • The structure of Aquifex aeolicus sulfide-quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
    • Marcia M, Ermler U, Peng G, Michel H (2009) The structure of Aquifex aeolicus sulfide-quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 106:9625-9630.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9625-9630
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4


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