메뉴 건너뛰기




Volumn 40, Issue 5, 2008, Pages 521-531

Cytochrome c oxidase: Exciting progress and remaining mysteries

Author keywords

Copper; Cytochrome; Energy coupling; Heme; Oxidase; Proton; Pump; Redox

Indexed keywords

COPPER; CYTOCHROME C OXIDASE; HEME; OXYGEN; PROTON; PROTON PUMP; WATER;

EID: 57049180108     PISSN: 0145479X     EISSN: 15736881     Source Type: Journal    
DOI: 10.1007/s10863-008-9181-7     Document Type: Review
Times cited : (237)

References (73)
  • 1
    • 0033788953 scopus 로고    scopus 로고
    • The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site
    • J Abramson S Riistama 2000 The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site Nature Struct Biol 7 910 917
    • (2000) Nature Struct Biol , vol.7 , pp. 910-917
    • Abramson, J.1    Riistama, S.2
  • 2
    • 0017883558 scopus 로고
    • Involvement of intramitochondrial protons in redox reactions of cytochrome a
    • VY Artzatbanov AA Konstantinov 1978 Involvement of intramitochondrial protons in redox reactions of cytochrome a FEBS Lett 87 180 185
    • (1978) FEBS Lett , vol.87 , pp. 180-185
    • Artzatbanov, V.Y.1    Konstantinov, A.A.2
  • 4
    • 33847272208 scopus 로고    scopus 로고
    • Exploring the proton pump mechanism of cytochrome c oxidase in real time
    • 8
    • I Belevich DA Bloch 2007 Exploring the proton pump mechanism of cytochrome c oxidase in real time Proc Natl Acad Sci U S A 104 8 2685 2690
    • (2007) Proc Natl Acad Sci U S a , vol.104 , pp. 2685-2690
    • Belevich, I.1    Bloch, D.A.2
  • 5
    • 0347004716 scopus 로고    scopus 로고
    • The catalytic cycle of cytochrome c oxidase is not the sum of its two halves
    • 2
    • D Bloch I Belevich 2004 The catalytic cycle of cytochrome c oxidase is not the sum of its two halves PNAS 101 2 529 533
    • (2004) PNAS , vol.101 , pp. 529-533
    • Bloch, D.1    Belevich, I.2
  • 6
    • 31044449343 scopus 로고    scopus 로고
    • Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidase
    • 2
    • G Brändén AS Pawate 2006 Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidase Proc Natl Acad Sci U S A 103 2 317 322
    • (2006) Proc Natl Acad Sci U S a , vol.103 , pp. 317-322
    • Brändén, G.1    Pawate, A.S.2
  • 7
    • 50949106489 scopus 로고    scopus 로고
    • The role of the conserved tryptophan272 of the Paracoccus denitrificans cytochrome c oxidase in proton pumping
    • 7-8
    • S de Vries 2008 The role of the conserved tryptophan272 of the Paracoccus denitrificans cytochrome c oxidase in proton pumping Biochim Biophys Acta 1777 7-8 925 928
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 925-928
    • De Vries, S.1
  • 8
    • 39949085428 scopus 로고    scopus 로고
    • Electrostatic control of proton pumping in cytochrome c oxidase
    • 3
    • E Fadda CH Yu 2008 Electrostatic control of proton pumping in cytochrome c oxidase Biochim Biophys Acta 1777 3 277 284
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 277-284
    • Fadda, E.1    Yu, C.H.2
  • 9
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • K Faxén G Gilderson 2005 A mechanistic principle for proton pumping by cytochrome c oxidase Nature 437 286
    • (2005) Nature , vol.437 , pp. 286
    • Faxén, K.1    Gilderson, G.2
  • 10
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • 96
    • S Ferguson-Miller GT Babcock 1996 Heme/copper terminal oxidases Chem Rev 7 96 2889 2907
    • (1996) Chem Rev , vol.7 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 11
    • 0028941458 scopus 로고
    • Possible proton relay pathways in cytochrome c oxidase
    • JR Fetter J Qian 1995 Possible proton relay pathways in cytochrome c oxidase Proc Natl Acad Sci U S A 92 1604 1608
    • (1995) Proc Natl Acad Sci U S a , vol.92 , pp. 1604-1608
    • Fetter, J.R.1    Qian, J.2
  • 12
    • 36049009410 scopus 로고    scopus 로고
    • Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans
    • 45
    • EA Gorbikova NP Belevich 2007 Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans Biochemistry 46 45 13141 13148
    • (2007) Biochemistry , vol.46 , pp. 13141-13148
    • Gorbikova, E.A.1    Belevich, N.P.2
  • 13
    • 0028219639 scopus 로고
    • Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site
    • S Hallén P Brzezinski 1994 Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site Biochemistry 33 1467 1472
    • (1994) Biochemistry , vol.33 , pp. 1467-1472
    • Hallén, S.1    Brzezinski, P.2
  • 14
    • 0034695481 scopus 로고    scopus 로고
    • Time dependence of the catalytic intermediates in cytochrome c oxidase
    • 3
    • S Han S Takahashi 2000 Time dependence of the catalytic intermediates in cytochrome c oxidase J Biol Chem 275 3 1910 1919
    • (2000) J Biol Chem , vol.275 , pp. 1910-1919
    • Han, S.1    Takahashi, S.2
  • 15
    • 33751569076 scopus 로고    scopus 로고
    • Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump
    • 47
    • D Han A Namslauer 2006 Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump Biochemistry 45 47 14064 14074
    • (2006) Biochemistry , vol.45 , pp. 14064-14074
    • Han, D.1    Namslauer, A.2
  • 16
    • 0032546595 scopus 로고    scopus 로고
    • Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FT-IR spectroscopy
    • P Hellwig J Behr 1998 Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FT-IR spectroscopy Biochemistry 37 7390 7399
    • (1998) Biochemistry , vol.37 , pp. 7390-7399
    • Hellwig, P.1    Behr, J.2
  • 17
    • 33845989511 scopus 로고    scopus 로고
    • Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases
    • 51
    • J Hemp DE Robinson 2006 Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases Biochemistry 45 51 15405 15410
    • (2006) Biochemistry , vol.45 , pp. 15405-15410
    • Hemp, J.1    Robinson, D.E.2
  • 18
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S Iwata C Ostermeier 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
  • 19
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen
    • A Jasaitis MI Verkhovsky 1999 Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen Biochemistry 38 2697 2706
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2
  • 20
    • 46349100115 scopus 로고    scopus 로고
    • Prevention of leak in the proton pump of cytochrome c oxidase
    • 7-8
    • VR Kaila M Verkhovsky 2008 Prevention of leak in the proton pump of cytochrome c oxidase Biochim Biophys Acta 1777 7-8 890 892
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 890-892
    • Kaila, V.R.1    Verkhovsky, M.2
  • 21
    • 44049096214 scopus 로고    scopus 로고
    • Glutamic acid 242 is a valve in the proton pump of cytochrome c oxidase
    • 17
    • VR Kaila MI Verkhovsky 2008 Glutamic acid 242 is a valve in the proton pump of cytochrome c oxidase Proc Natl Acad Sci U S A 105 17 6255 6259
    • (2008) Proc Natl Acad Sci U S a , vol.105 , pp. 6255-6259
    • Kaila, V.R.1    Verkhovsky, M.I.2
  • 22
    • 0031688652 scopus 로고    scopus 로고
    • Electrical current generation and proton pumping catalyzed by the ba3-type cytochrome c oxidase from Thermus thermophilus
    • A Kannt T Soulimane 1998 Electrical current generation and proton pumping catalyzed by the ba3-type cytochrome c oxidase from Thermus thermophilus FEBS 434 17 22
    • (1998) FEBS , vol.434 , pp. 17-22
    • Kannt, A.1    Soulimane, T.2
  • 23
    • 27844524873 scopus 로고    scopus 로고
    • Oxygen activation mechanism at the binuclear site of heme-copper oxidase superfamily as revealed by time-resolved resonance Raman spectroscopy
    • T Kitagawa T Ogura 1997 Oxygen activation mechanism at the binuclear site of heme-copper oxidase superfamily as revealed by time-resolved resonance Raman spectroscopy Prog Inorg Chem 45 431 479
    • (1997) Prog Inorg Chem , vol.45 , pp. 431-479
    • Kitagawa, T.1    Ogura, T.2
  • 24
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • AA Konstantinov S Siletsky 1997 The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer Proc Natl Acad Sci U S A 94 9085 9090
    • (1997) Proc Natl Acad Sci U S a , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2
  • 25
    • 0034696637 scopus 로고    scopus 로고
    • Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a
    • H-m Lee TK Das 2000 Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a Biochemistry 39 2989 2996
    • (2000) Biochemistry , vol.39 , pp. 2989-2996
    • H-M, L.1    Das, T.K.2
  • 26
    • 46349095702 scopus 로고    scopus 로고
    • Impaired proton pumping in cytochrome c oxidase upon structural alteration of the D pathway
    • 7-8
    • H Lepp L Salomonsson 2008 Impaired proton pumping in cytochrome c oxidase upon structural alteration of the D pathway Biochim Biophys Acta 1777 7-8 897 903
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 897-903
    • Lepp, H.1    Salomonsson, L.2
  • 27
    • 42449087250 scopus 로고    scopus 로고
    • Charge transfer in the K proton pathway linked to electron transfer to the catalytic site in cytochrome c oxidase
    • 17
    • H Lepp E Svahn 2008 Charge transfer in the K proton pathway linked to electron transfer to the catalytic site in cytochrome c oxidase Biochemistry 47 17 4929 4935
    • (2008) Biochemistry , vol.47 , pp. 4929-4935
    • Lepp, H.1    Svahn, E.2
  • 28
    • 42349083650 scopus 로고    scopus 로고
    • Crystallographic studies of Xe and Kr binding within the large internal cavity of cytochrome ba3 from Thermus thermophilus: Structural analysis and role of oxygen transport channels in the heme-Cu oxidases
    • 16
    • VM Luna Y Chen 2008 Crystallographic studies of Xe and Kr binding within the large internal cavity of cytochrome ba3 from Thermus thermophilus: structural analysis and role of oxygen transport channels in the heme-Cu oxidases Biochemistry 47 16 4657 4665
    • (2008) Biochemistry , vol.47 , pp. 4657-4665
    • Luna, V.M.1    Chen, Y.2
  • 29
    • 34249944838 scopus 로고    scopus 로고
    • A histidine residue acting as a controlling site for dioxygen reduction and proton pumping by cytochrome c oxidase
    • 19
    • K Muramoto K Hirata 2007 A histidine residue acting as a controlling site for dioxygen reduction and proton pumping by cytochrome c oxidase Proc Natl Acad Sci U S A 104 19 7881 7886
    • (2007) Proc Natl Acad Sci U S a , vol.104 , pp. 7881-7886
    • Muramoto, K.1    Hirata, K.2
  • 30
    • 0020967882 scopus 로고
    • Hydrogen bonded chain mechanisms for proton conduction and proton pumping
    • JF Nagle S Tristam-Nagle 1983 Hydrogen bonded chain mechanisms for proton conduction and proton pumping J Membr Biol 74 1 14
    • (1983) J Membr Biol , vol.74 , pp. 1-14
    • Nagle, J.F.1    Tristam-Nagle, S.2
  • 31
    • 0037452497 scopus 로고    scopus 로고
    • Intramolecular proton-transfer reactions in a membrane-bound proton pump: The effect of pH on the peroxy to ferryl transition in cytochrome c oxidase
    • A Namslauer A Aagaard 2003 Intramolecular proton-transfer reactions in a membrane-bound proton pump: the effect of pH on the peroxy to ferryl transition in cytochrome c oxidase Bichemistry 42 1488 1498
    • (2003) Bichemistry , vol.42 , pp. 1488-1498
    • Namslauer, A.1    Aagaard, A.2
  • 32
    • 0346734127 scopus 로고    scopus 로고
    • Redox-coupled proton translocation in biological systems: Proton shuttling in cytochrome c oxidase
    • 26
    • A Namslauer A Pawate 2003 Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase Proc Natl Acad Sci U S A 100 26 15543 15547
    • (2003) Proc Natl Acad Sci U S a , vol.100 , pp. 15543-15547
    • Namslauer, A.1    Pawate, A.2
  • 33
    • 0035823117 scopus 로고    scopus 로고
    • Perfusion-induced redox differences in cytochrome c oxidase: ATR/FT-IR spectroscopy
    • RM Nyquist D Heitbrink 2001 Perfusion-induced redox differences in cytochrome c oxidase: ATR/FT-IR spectroscopy FEBS Letters 505 63 67
    • (2001) FEBS Letters , vol.505 , pp. 63-67
    • Nyquist, R.M.1    Heitbrink, D.2
  • 34
    • 0001068250 scopus 로고
    • Time-resolved resonance Raman elucidation of the pathway for dioxygen reduction by cytochrome c oxidase'
    • T Ogura S Takahashi 1993 Time-resolved resonance Raman elucidation of the pathway for dioxygen reduction by cytochrome c oxidase' J Am Chem Soc 115 8527 8536
    • (1993) J Am Chem Soc , vol.115 , pp. 8527-8536
    • Ogura, T.1    Takahashi, S.2
  • 35
    • 33646268674 scopus 로고    scopus 로고
    • Monte Carlo simulations of proton pumps: On the working principles of the biological valve that controls proton pumping in cytochrome c oxidase
    • 17
    • MH Olsson A Warshel 2006 Monte Carlo simulations of proton pumps: on the working principles of the biological valve that controls proton pumping in cytochrome c oxidase Proc Natl Acad Sci USA 103 17 6500 6505
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6500-6505
    • Olsson, M.H.1    Warshel, A.2
  • 36
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment
    • C Ostermeier A Harrenga 1997 Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment Proc Natl Acad Sci U S A 94 10547 10553
    • (1997) Proc Natl Acad Sci U S a , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2
  • 37
    • 0037069405 scopus 로고    scopus 로고
    • A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping
    • AS Pawate 2002 A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping Biochemistry 41 13417 13423
    • (2002) Biochemistry , vol.41 , pp. 13417-13423
    • Pawate, A.S.1
  • 38
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evaluation of haem-copper oxygen reductases
    • MM Pereira M Santana 2001 A novel scenario for the evaluation of haem-copper oxygen reductases Biochim Biophys Acta 1505 185 208
    • (2001) Biochim Biophys Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2
  • 39
    • 46349107814 scopus 로고    scopus 로고
    • Looking for the minimum common denominator in haem-copper oxygen reductases: Towards a unified catalytic mechanism
    • 7-8
    • MM Pereira FL Sousa 2008 Looking for the minimum common denominator in haem-copper oxygen reductases: towards a unified catalytic mechanism Biochim Biophys Acta 1777 7-8 929 934
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 929-934
    • Pereira, M.M.1    Sousa, F.L.2
  • 40
    • 0034643820 scopus 로고    scopus 로고
    • Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans
    • 23
    • U Pfitzner K Hoffmeier 2000 Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans Biochemistry 39 23 6756 6762
    • (2000) Biochemistry , vol.39 , pp. 6756-6762
    • Pfitzner, U.1    Hoffmeier, K.2
  • 41
    • 45549107077 scopus 로고    scopus 로고
    • Electrostatic basis for the unidirectionality of the primary proton transfer in cytochrome c oxidase
    • 22
    • AV Pisliakov PK Sharma 2008 Electrostatic basis for the unidirectionality of the primary proton transfer in cytochrome c oxidase Proc Natl Acad Sci U S A 105 22 7726 7731
    • (2008) Proc Natl Acad Sci U S a , vol.105 , pp. 7726-7731
    • Pisliakov, A.V.1    Sharma, P.K.2
  • 42
    • 2442616154 scopus 로고    scopus 로고
    • Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating
    • DM Popovic AA Stuchebrukhov 2004 Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: coulomb pump model with kinetic gating FEBS Lett 566 126 130
    • (2004) FEBS Lett , vol.566 , pp. 126-130
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 43
    • 13444305368 scopus 로고    scopus 로고
    • Proton exit channels in bovine cytochrome c oxidase
    • DM Popovic AA Stuchebrukhov 2005 Proton exit channels in bovine cytochrome c oxidase J Phys Chem B 109 1999 2006
    • (2005) J Phys Chem B , vol.109 , pp. 1999-2006
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 44
    • 0034711407 scopus 로고    scopus 로고
    • Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244
    • DA Proshlyakov MA Pressler 2000 Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244 Science 290 1588 1591
    • (2000) Science , vol.290 , pp. 1588-1591
    • Proshlyakov, D.A.1    Pressler, M.A.2
  • 45
    • 33750807024 scopus 로고    scopus 로고
    • Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
    • 44
    • L Qin C Hiser 2006 Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase Proc Natl Acad Sci U S A 103 44 16117 16122
    • (2006) Proc Natl Acad Sci U S a , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2
  • 46
    • 34249668338 scopus 로고    scopus 로고
    • Crystallographic location and mutational analysis of zn and cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome C oxidase
    • 21
    • L Qin DA Mills 2007 Crystallographic location and mutational analysis of zn and cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome C oxidase Biochemistry 46 21 6239 6248
    • (2007) Biochemistry , vol.46 , pp. 6239-6248
    • Qin, L.1    Mills, D.A.2
  • 47
    • 0028813330 scopus 로고
    • Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases
    • PR Rich 1995 Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases Aust J Plant Physiol 22 479 486
    • (1995) Aust J Plant Physiol , vol.22 , pp. 479-486
    • Rich, P.R.1
  • 48
    • 0030592181 scopus 로고    scopus 로고
    • Coupling of charge and proton movement in cytochrome c oxidase
    • PR Rich B Meunier 1996 Coupling of charge and proton movement in cytochrome c oxidase Biochim Biophys Acta 1275 91 95
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 91-95
    • Rich, P.R.1    Meunier, B.2
  • 49
    • 0031744887 scopus 로고    scopus 로고
    • Protonmotive mechanism of haem-copper oxidases
    • 1
    • PR Rich S Jünemann 1997 Protonmotive mechanism of haem-copper oxidases J Bioenerg Biomembr 30 1 131 137
    • (1997) J Bioenerg Biomembr , vol.30 , pp. 131-137
    • Rich, P.R.1    Jünemann, S.2
  • 50
    • 0031559894 scopus 로고    scopus 로고
    • Bound water in the proton translocation mechanism of the heme-copper oxidases
    • 2
    • S Riistama G Hummer 1997 Bound water in the proton translocation mechanism of the heme-copper oxidases FEBS Lett 414 2 275 280
    • (1997) FEBS Lett , vol.414 , pp. 275-280
    • Riistama, S.1    Hummer, G.2
  • 51
    • 29144503674 scopus 로고    scopus 로고
    • The timing of proton migration in membrane-reconstituted cytochrome c oxidase
    • 49
    • L Salomonsson K Faxen 2005 The timing of proton migration in membrane-reconstituted cytochrome c oxidase Proc Natl Acad Sci U S A 102 49 17624 17629
    • (2005) Proc Natl Acad Sci U S a , vol.102 , pp. 17624-17629
    • Salomonsson, L.1    Faxen, K.2
  • 52
    • 34247180567 scopus 로고    scopus 로고
    • The proton pumping pathway of bovine heart cytochrome c oxidase
    • 10
    • K Shimokata Y Katayama 2007 The proton pumping pathway of bovine heart cytochrome c oxidase Proc Natl Acad Sci U S A 104 10 4200 4205
    • (2007) Proc Natl Acad Sci U S a , vol.104 , pp. 4200-4205
    • Shimokata, K.1    Katayama, Y.2
  • 53
    • 33947602374 scopus 로고    scopus 로고
    • Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase
    • 6
    • K Shinzawa-Itoh H Aoyama 2007 Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase EMBO J 26 6 1713 1725
    • (2007) EMBO J , vol.26 , pp. 1713-1725
    • Shinzawa-Itoh, K.1    Aoyama, H.2
  • 54
    • 34548170174 scopus 로고    scopus 로고
    • Energy diagrams and mechanism for proton pumping in cytochrome c oxidase
    • 9
    • PE Siegbahn MR Blomberg 2007 Energy diagrams and mechanism for proton pumping in cytochrome c oxidase Biochim Biophys Acta 1767 9 1143 1156
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1143-1156
    • Siegbahn, P.E.1    Blomberg, M.R.2
  • 55
    • 10644252589 scopus 로고    scopus 로고
    • Transmembrane charge separation during the Ferryl-oxo Ø oxidized transition in a nonpumping mutant of cytochrome c oxidase
    • 50
    • SA Siletsky AS Pawate 2004 Transmembrane charge separation during the Ferryl-oxo Ø oxidized transition in a nonpumping mutant of cytochrome c oxidase J Biol Chem 279 50 52558 52565
    • (2004) J Biol Chem , vol.279 , pp. 52558-52565
    • Siletsky, S.A.1    Pawate, A.S.2
  • 56
    • 36549060589 scopus 로고    scopus 로고
    • Time-resolved single-turnover of ba3 oxidase from Thermus thermophilus
    • 12
    • SA Siletsky I Belevich 2007 Time-resolved single-turnover of ba3 oxidase from Thermus thermophilus Biochim Biophys Acta 1767 12 1383 1392
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1383-1392
    • Siletsky, S.A.1    Belevich, I.2
  • 57
    • 0033602933 scopus 로고    scopus 로고
    • Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during Oxo-Ferryl formation
    • IA Smirnova P Ädelroth 1999 Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during Oxo-Ferryl formation Biochemistry 38 6826 6833
    • (1999) Biochemistry , vol.38 , pp. 6826-6833
    • Smirnova, I.A.1    Ädelroth, P.2
  • 58
    • 0034678612 scopus 로고    scopus 로고
    • Structure and mechanism of the aberrant ba3-cytochrome c oxidase from Thermus thermophilus
    • 8
    • T Soulimane G Buse 2000 Structure and mechanism of the aberrant ba3-cytochrome c oxidase from Thermus thermophilus EMBO J 19 8 1766 1776
    • (2000) EMBO J , vol.19 , pp. 1766-1776
    • Soulimane, T.1    Buse, G.2
  • 59
    • 49349116297 scopus 로고    scopus 로고
    • Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme
    • R Sugitani ES Medvedev 2008 Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme Biochim Biophys Acta 1777 1129 1139
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1129-1139
    • Sugitani, R.1    Medvedev, E.S.2
  • 60
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • M Svensson-Ek J Abramson 2002 The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides J Mol Biol 321 329 339
    • (2002) J Mol Biol , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2
  • 61
    • 0029652024 scopus 로고
    • Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å
    • T Tsukihara H Aoyama 1995 Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å Science 269 1069 1074
    • (1995) Science , vol.269 , pp. 1069-1074
    • Tsukihara, T.1    Aoyama, H.2
  • 62
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å
    • T Tsukihara H Aoyama 1996 The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å Science 272 1136 1144
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1    Aoyama, H.2
  • 63
    • 33746928351 scopus 로고    scopus 로고
    • Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286
    • 19
    • AS Vakkasoglu JE Morgan 2006 Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286 FEBS Lett 580 19 4613 4617
    • (2006) FEBS Lett , vol.580 , pp. 4613-4617
    • Vakkasoglu, A.S.1    Morgan, J.E.2
  • 64
    • 0027393739 scopus 로고
    • Resolution of the reaction sequence during the reduction of O2 by cytochrome oxidase
    • C Varotsis Y Zhang 1993 Resolution of the reaction sequence during the reduction of O2 by cytochrome oxidase Proc Natl Acad Sci U S A 90 237 241
    • (1993) Proc Natl Acad Sci U S a , vol.90 , pp. 237-241
    • Varotsis, C.1    Zhang, Y.2
  • 65
    • 0026496717 scopus 로고
    • Intramolecular electron transfer in cytochrome c oxidase: A cascade of equilibria
    • MI Verkhovsky JE Morgan 1992 Intramolecular electron transfer in cytochrome c oxidase: a cascade of equilibria Biochemistry 31 11860 11863
    • (1992) Biochemistry , vol.31 , pp. 11860-11863
    • Verkhovsky, M.I.1    Morgan, J.E.2
  • 66
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • MI Verkhovsky JE Morgan 1994 Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase Biochemistry 33 3079 3086
    • (1994) Biochemistry , vol.33 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2
  • 67
    • 0031028098 scopus 로고    scopus 로고
    • Translocation of electrical charge during a single turnover of cytochrome-c oxidase
    • MI Verkhovsky JE Morgan 1997 Translocation of electrical charge during a single turnover of cytochrome-c oxidase Biochim Biophys Acta 1318 6 10
    • (1997) Biochim Biophys Acta , vol.1318 , pp. 6-10
    • Verkhovsky, M.I.1    Morgan, J.E.2
  • 68
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • M Wikström 1977 Proton pump coupled to cytochrome c oxidase in mitochondria Nature 266 271 273
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.1
  • 69
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • 10
    • M Wikstrom MI Verkhovsky 2007 Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases Biochim Biophys Acta 1767 10 1200 1214
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1200-1214
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 70
    • 0037726809 scopus 로고    scopus 로고
    • Water-gated mechanism of proton translocation by cytochrome c oxidase
    • M Wikström MI Verkhovsky 2003 Water-gated mechanism of proton translocation by cytochrome c oxidase Biochim Biophys Acta 1604 61 65
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 61-65
    • Wikström, M.1    Verkhovsky, M.I.2
  • 71
    • 33947280355 scopus 로고    scopus 로고
    • Storage of an excess proton in the hydrogen-bonded network of the d-pathway of cytochrome C oxidase: Identification of a protonated water cluster
    • 10
    • J Xu MA Sharpe 2007 Storage of an excess proton in the hydrogen-bonded network of the d-pathway of cytochrome C oxidase: identification of a protonated water cluster J Am Chem Soc 129 10 2910 2913
    • (2007) J Am Chem Soc , vol.129 , pp. 2910-2913
    • Xu, J.1    Sharpe, M.A.2
  • 72
    • 0033741298 scopus 로고    scopus 로고
    • X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase
    • S Yoshikawa K Shinzawa-Itoh 2000 X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase J Inorg Biochem 82 1 7
    • (2000) J Inorg Biochem , vol.82 , pp. 1-7
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2
  • 73
    • 0037422418 scopus 로고    scopus 로고
    • Computer simulation of water in cytochrome c oxidase
    • X Zheng DM Medvedev 2003 Computer simulation of water in cytochrome c oxidase Biochim Biophys Acta 1557 99 107
    • (2003) Biochim Biophys Acta , vol.1557 , pp. 99-107
    • Zheng, X.1    Medvedev, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.