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Volumn 10, Issue 1, 2008, Pages 1-29

Molecular mechanism of proton translocation by cytochrome c oxidase

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; OXYGEN; PROTON PUMP; REACTIVE OXYGEN METABOLITE; WATER;

EID: 36148938761     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2007.1705     Document Type: Review
Times cited : (125)

References (271)
  • 3
    • 0028925948 scopus 로고
    • Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides
    • Ädelroth P, Brzezinski P, and Malmström BG. Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 34: 2844-2849, 1995.
    • (1995) Biochemistry , vol.34 , pp. 2844-2849
    • Ädelroth, P.1    Brzezinski, P.2    Malmström, B.G.3
  • 4
    • 0032487395 scopus 로고    scopus 로고
    • Factors determining electron-transfer rates in cytochrome c oxidase: Investigation of the oxygen reaction in the R. sphaeroides enzyme
    • Ädelroth P, Ek M, and Brzezinski P. Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides enzyme. Biochim Biophys Acta 1367: 107-117, 1998.
    • (1998) Biochim Biophys Acta , vol.1367 , pp. 107-117
    • Ädelroth, P.1    Ek, M.2    Brzezinski, P.3
  • 5
    • 0343580460 scopus 로고    scopus 로고
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen. Biochemistry 36: 13824-13829, 1997.
    • (1997) Biochemistry , vol.36 , pp. 13824-13829
    • Ädelroth, P.1    Ek, M.S.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 6
    • 0032562214 scopus 로고    scopus 로고
    • Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides
    • Ädelroth P, Gennis RB, and Brzezinski P. Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides. Biochemistry 37: 2470-2476, 1998.
    • (1998) Biochemistry , vol.37 , pp. 2470-2476
    • Ädelroth, P.1    Gennis, R.B.2    Brzezinski, P.3
  • 7
    • 11744384413 scopus 로고
    • The Grotthuss mechanism
    • Agmon N. The Grotthuss mechanism. Chem Phys Lett 244: 456-462, 1995.
    • (1995) Chem Phys Lett , vol.244 , pp. 456-462
    • Agmon, N.1
  • 8
    • 0019484649 scopus 로고
    • 3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex
    • 3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex. Proc Natl Acad Sci U S A 78: 234-237, 1981.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 234-237
    • Alben, J.O.1    Moh, P.P.2    Fiamingo, F.G.3    Altschuld, R.A.4
  • 9
    • 0001383847 scopus 로고
    • The aerobic respiratory chain of Escherichia coli
    • Anraku Y and Gennis RB. The aerobic respiratory chain of Escherichia coli. Trends Biochem Sci 12: 262-266, 1987.
    • (1987) Trends Biochem Sci , vol.12 , pp. 262-266
    • Anraku, Y.1    Gennis, R.B.2
  • 10
    • 0020479091 scopus 로고
    • Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c
    • Antalis TM and Palmer G. Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c. J Biol Chem 257: 6194-6206, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 6194-6206
    • Antalis, T.M.1    Palmer, G.2
  • 11
    • 0026457361 scopus 로고
    • A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase
    • Antholine WE, Kastrau DH, Steffens GC, Buse G, Zumft WG, and Kroneck PM. A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase. Eur J Biochem 209: 875-881, 1992.
    • (1992) Eur J Biochem , vol.209 , pp. 875-881
    • Antholine, W.E.1    Kastrau, D.H.2    Steffens, G.C.3    Buse, G.4    Zumft, W.G.5    Kroneck, P.M.6
  • 13
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: Metabolism, oxidative stress, and signal transduction
    • Apel K and Hirt H. Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol 55: 373-399, 2004.
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 14
    • 0032031485 scopus 로고    scopus 로고
    • 3,5-Diiodothyronine binds to subunit Va of cytochrome c oxidase and abolishes the allosteric inhibition of respiration by ATP
    • Arnold S, Goglia F, and Kadenbach B. 3,5-Diiodothyronine binds to subunit Va of cytochrome c oxidase and abolishes the allosteric inhibition of respiration by ATP. Eur J Biochem 252: 325-330, 1998.
    • (1998) Eur J Biochem , vol.252 , pp. 325-330
    • Arnold, S.1    Goglia, F.2    Kadenbach, B.3
  • 15
    • 0017883558 scopus 로고
    • Involvement of intramitochondrial protons in redox reactions of cytochrome a
    • Artzatbanov VY, Konstantinov AA, and Skulachev VP. Involvement of intramitochondrial protons in redox reactions of cytochrome a. FEBS Lett 87: 180-185, 1978.
    • (1978) FEBS Lett , vol.87 , pp. 180-185
    • Artzatbanov, V.Y.1    Konstantinov, A.A.2    Skulachev, V.P.3
  • 16
    • 0021099512 scopus 로고
    • Redox-linked hydrogen bond strength changes in cytochrome a: Implications for a cytochrome oxidase proton pump
    • Babcock GT and Callahan PM. Redox-linked hydrogen bond strength changes in cytochrome a: implications for a cytochrome oxidase proton pump. Biochemistry 22: 2314-2319, 1983.
    • (1983) Biochemistry , vol.22 , pp. 2314-2319
    • Babcock, G.T.1    Callahan, P.M.2
  • 18
    • 0017049582 scopus 로고
    • Electronic state of heme in cytochrome oxidase, I: Magnetic circular dichroism of the isolated enzyme and its derivatives
    • Babcock GT, Vickery LE, and Palmer G. Electronic state of heme in cytochrome oxidase, I: Magnetic circular dichroism of the isolated enzyme and its derivatives. J Biol Chem 251: 7907-7919, 1976.
    • (1976) J Biol Chem , vol.251 , pp. 7907-7919
    • Babcock, G.T.1    Vickery, L.E.2    Palmer, G.3
  • 19
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock GT and Wikström M. Oxygen activation and the conservation of energy in cell respiration. Nature 356: 301-309, 1992.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 20
    • 0023096414 scopus 로고
    • The reaction of cytochrome oxidase with cyanide: Preparation of the rapidly reacting form and its conversion to the slowly reacting form
    • Baker GM, Noguchi M, and Palmer G. The reaction of cytochrome oxidase with cyanide: preparation of the rapidly reacting form and its conversion to the slowly reacting form. J Biol Chem 262: 595-604, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 595-604
    • Baker, G.M.1    Noguchi, M.2    Palmer, G.3
  • 21
    • 0017285154 scopus 로고
    • Kinetic studies on cytochrome c oxidase by combined EPR and reflectance spectroscopy after rapid freezing
    • Beinert H, Hansen RE, and Hartzell CR. Kinetic studies on cytochrome c oxidase by combined EPR and reflectance spectroscopy after rapid freezing. Biochim Biophys Acta 423: 339-355, 1976.
    • (1976) Biochim Biophys Acta , vol.423 , pp. 339-355
    • Beinert, H.1    Hansen, R.E.2    Hartzell, C.R.3
  • 22
    • 0008426653 scopus 로고
    • Properties of copper associated with cytochrome oxidase as studied by paramagnetic resonance spectroscopy
    • Beinert H, Wharton DC, Griffiths DE, and Sands RH. Properties of copper associated with cytochrome oxidase as studied by paramagnetic resonance spectroscopy. J Biol Chem 237: 2337-2354, 1962.
    • (1962) J Biol Chem , vol.237 , pp. 2337-2354
    • Beinert, H.1    Wharton, D.C.2    Griffiths, D.E.3    Sands, R.H.4
  • 24
    • 24044519364 scopus 로고    scopus 로고
    • Oxygenated complex of cytochrome bd from Escherichia coli: Stability and photolability
    • Belevich I, Borisov VB, Konstantinov AA, and Verkhovsky MI. Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability. FEBS Lett 579: 4567-4570, 2005.
    • (2005) FEBS Lett , vol.579 , pp. 4567-4570
    • Belevich, I.1    Borisov, V.B.2    Konstantinov, A.A.3    Verkhovsky, M.I.4
  • 25
    • 33645461637 scopus 로고    scopus 로고
    • Proton-coupled electron equilibrium in soluble and membrane-bound cytochrome c oxidase from Paracoccus denitrificans
    • Belevich I, Tuukkanen A, Wikström M, and Verkhovsky MI. Proton-coupled electron equilibrium in soluble and membrane-bound cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 45: 4000-4006, 2006.
    • (2006) Biochemistry , vol.45 , pp. 4000-4006
    • Belevich, I.1    Tuukkanen, A.2    Wikström, M.3    Verkhovsky, M.I.4
  • 26
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • Belevich I, Verkhovsky MI, and Wikström M. Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase. Nature 440: 829-832, 2006.
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikström, M.3
  • 28
    • 0037066090 scopus 로고    scopus 로고
    • Electron transport routes in whole cells of Synechocystis sp. strain PCC 6803: The role of the cytochrome bd-type oxidase
    • Berry S, Schneider D, Vermaas WF, and Rögner M. Electron transport routes in whole cells of Synechocystis sp. strain PCC 6803: the role of the cytochrome bd-type oxidase. Biochemistry 41: 3422-3429, 2002.
    • (2002) Biochemistry , vol.41 , pp. 3422-3429
    • Berry, S.1    Schneider, D.2    Vermaas, W.F.3    Rögner, M.4
  • 29
    • 0020490631 scopus 로고
    • Cytochrome c oxidase binding of hydrogen peroxide
    • Bickar D, Bonaventura J, and Bonaventura C. Cytochrome c oxidase binding of hydrogen peroxide. Biochemistry 21: 2661-2666, 1982.
    • (1982) Biochemistry , vol.21 , pp. 2661-2666
    • Bickar, D.1    Bonaventura, J.2    Bonaventura, C.3
  • 30
    • 0026038522 scopus 로고
    • Studies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase
    • Blackmore RS, Greenwood C, and Gibson QH. Studies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase. J Biol Chem 266: 19245-19249, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 19245-19249
    • Blackmore, R.S.1    Greenwood, C.2    Gibson, Q.H.3
  • 31
    • 0022967236 scopus 로고
    • Spectroelectrochemical study of cytochrome c oxidase: PH and temperature dependences of the cytochrome potentials: characterization of site-site interactions
    • Blair DF, Ellis WR Jr, Wang H, Gray HB, and Chan SI. Spectroelectrochemical study of cytochrome c oxidase: pH and temperature dependences of the cytochrome potentials: characterization of site-site interactions. J Biol Chem 261: 11524-11537, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 11524-11537
    • Blair, D.F.1    Ellis Jr, W.R.2    Wang, H.3    Gray, H.B.4    Chan, S.I.5
  • 32
    • 0000806437 scopus 로고
    • Mechanism of cytochrome c oxidase-catalyzed dioxygen reduction at low-temperatures: Evidence for 2 intermediates at the 3-electron level and entropic promotion of the bond-breaking step
    • Blair DF, Witt SN, and Chan SI. Mechanism of cytochrome c oxidase-catalyzed dioxygen reduction at low-temperatures: evidence for 2 intermediates at the 3-electron level and entropic promotion of the bond-breaking step. J Am Chem Soc 107: 7389-7399, 1985.
    • (1985) J Am Chem Soc , vol.107 , pp. 7389-7399
    • Blair, D.F.1    Witt, S.N.2    Chan, S.I.3
  • 35
    • 0029910514 scopus 로고    scopus 로고
    • - stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells
    • - stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells. J Bacteriol 178: 6233-6237, 1996.
    • (1996) J Bacteriol , vol.178 , pp. 6233-6237
    • Bogachev, A.V.1    Murtazina, R.A.2    Skulachev, V.P.3
  • 37
    • 18844479874 scopus 로고    scopus 로고
    • Water-hydroxide exchange reactions at the catalytic site of hemecopper oxidases
    • Bränden M, Namslauer A, Hansson O, Aasa R, and Brzezinski P. Water-hydroxide exchange reactions at the catalytic site of hemecopper oxidases. Biochemistry 42: 13178-13184, 2003.
    • (2003) Biochemistry , vol.42 , pp. 13178-13184
    • Bränden, M.1    Namslauer, A.2    Hansson, O.3    Aasa, R.4    Brzezinski, P.5
  • 39
    • 0037015164 scopus 로고    scopus 로고
    • The entry point of the K-proton-transfer pathway in cytochrome c oxidase
    • Bränden M, Tomson F, Gennis RB, and Brzezinski P. The entry point of the K-proton-transfer pathway in cytochrome c oxidase. Biochemistry 41: 10794-10798, 2002.
    • (2002) Biochemistry , vol.41 , pp. 10794-10798
    • Bränden, M.1    Tomson, F.2    Gennis, R.B.3    Brzezinski, P.4
  • 40
    • 4243181574 scopus 로고    scopus 로고
    • Internal electron-transfer reactions in cytochrome c oxidase
    • Brzezinski P. Internal electron-transfer reactions in cytochrome c oxidase. Biochemistry 35: 5611-5615, 1996.
    • (1996) Biochemistry , vol.35 , pp. 5611-5615
    • Brzezinski, P.1
  • 41
    • 4243181574 scopus 로고    scopus 로고
    • Internal electron-transfer reactions in cytochrome c oxidase
    • Brzezinski P. Internal electron-transfer reactions in cytochrome c oxidase. Biochemistry 35: 5611-5615, 1996.
    • (1996) Biochemistry , vol.35 , pp. 5611-5615
    • Brzezinski, P.1
  • 42
    • 0041765700 scopus 로고    scopus 로고
    • Redox-driven proton pumping by heme-copper oxidases
    • Brzezinski P and Larsson G. Redox-driven proton pumping by heme-copper oxidases. Biochim Biophys Acta 1605: 1-13, 2003.
    • (2003) Biochim Biophys Acta , vol.1605 , pp. 1-13
    • Brzezinski, P.1    Larsson, G.2
  • 43
    • 0032924497 scopus 로고    scopus 로고
    • Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase
    • Buse G, Soulimane T, Dewor M, Meyer HE, and Blüggel M. Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase. Protein Sci 8: 985-990, 1999.
    • (1999) Protein Sci , vol.8 , pp. 985-990
    • Buse, G.1    Soulimane, T.2    Dewor, M.3    Meyer, H.E.4    Blüggel, M.5
  • 44
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell GW, Louie GV, and Brayer GD. High-resolution three-dimensional structure of horse heart cytochrome c. J Mol Biol 214: 585-595, 1990.
    • (1990) J Mol Biol , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 45
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas E and Davies KJ. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 29: 222-230, 2000.
    • (2000) Free Radic Biol Med , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 46
    • 0028137093 scopus 로고
    • The cytochrome oxidase superfamily of redox-driven proton pumps
    • Calhoun MW, Thomas JW, and Gennis RB. The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem Sci 19: 325-330, 1994.
    • (1994) Trends Biochem Sci , vol.19 , pp. 325-330
    • Calhoun, M.W.1    Thomas, J.W.2    Gennis, R.B.3
  • 47
    • 0021107158 scopus 로고
    • Origin of the cytochrome a absorption red shift: A pH-dependent interaction between its heme a formyl and protein in cytochrome oxidase
    • Callahan PM and Babcock GT. Origin of the cytochrome a absorption red shift: a pH-dependent interaction between its heme a formyl and protein in cytochrome oxidase. Biochemistry 22: 452-461, 1983.
    • (1983) Biochemistry , vol.22 , pp. 452-461
    • Callahan, P.M.1    Babcock, G.T.2
  • 48
    • 0026615058 scopus 로고
    • 3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase: The coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast
    • 3 of Rhodobacter sphaeroides as a model for mitochondrial cytochrome c oxidase: the coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast. J Biol Chem 267: 24273-24278, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 24273-24278
    • Cao, J.1    Hosler, J.2    Shapleigh, J.3    Revzin, A.4    Ferguson-Miller, S.5
  • 49
    • 0025801345 scopus 로고
    • The gene encoding cytochrome c oxidase subunit II from Rhodobacter sphaeroides: Comparison of the deduced amino acid sequence with sequences of corresponding peptides from other species
    • Cao J, Shapleigh J, Gennis R, Revzin A, and Ferguson-Miller S. The gene encoding cytochrome c oxidase subunit II from Rhodobacter sphaeroides: comparison of the deduced amino acid sequence with sequences of corresponding peptides from other species. Gene 101: 133-137, 1991.
    • (1991) Gene , vol.101 , pp. 133-137
    • Cao, J.1    Shapleigh, J.2    Gennis, R.3    Revzin, A.4    Ferguson-Miller, S.5
  • 50
    • 0025322981 scopus 로고
    • Structure and function of cytochrome c oxidase
    • Capaldi RA. Structure and function of cytochrome c oxidase. Annu Rev Biochem 59: 569-596, 1990.
    • (1990) Annu Rev Biochem , vol.59 , pp. 569-596
    • Capaldi, R.A.1
  • 51
    • 0031015579 scopus 로고    scopus 로고
    • Redox-linked protolytic reactions in soluble cytochrome-c oxidase from beef-heart mitochondria: Redox Bohr effects
    • Capitanio N, Vygodina TV, Capitanio G, Konstantinov AA, Nicholls P, and Papa S. Redox-linked protolytic reactions in soluble cytochrome-c oxidase from beef-heart mitochondria: redox Bohr effects. Biochim Biophys Acta 1318: 255-265, 1997.
    • (1997) Biochim Biophys Acta , vol.1318 , pp. 255-265
    • Capitanio, N.1    Vygodina, T.V.2    Capitanio, G.3    Konstantinov, A.A.4    Nicholls, P.5    Papa, S.6
  • 52
    • 0037184987 scopus 로고    scopus 로고
    • Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. identification of two new subunits
    • Carroll J, Shannon RJ, Fearnley IM, Walker JE, and Hirst J. Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. identification of two new subunits. J Biol Chem 277: 50311-50317, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 50311-50317
    • Carroll, J.1    Shannon, R.J.2    Fearnley, I.M.3    Walker, J.E.4    Hirst, J.5
  • 53
    • 0018791868 scopus 로고
    • Limited-turnover studies on proton translocation in reconstituted cytochrome c oxidase-containing vesicles
    • Casey RP, Chappell JB, and Azzi A. Limited-turnover studies on proton translocation in reconstituted cytochrome c oxidase-containing vesicles. Biochem J 182: 149-156, 1979.
    • (1979) Biochem J , vol.182 , pp. 149-156
    • Casey, R.P.1    Chappell, J.B.2    Azzi, A.3
  • 54
    • 0016819667 scopus 로고
    • Heme A of cytochrome c oxidase; structure and properties: Comparisons with heme B, heme-C and heme-S and derivatives
    • Caughey WS, Smythe GA, Okeeffe DH, Maskasky JE, and Smith ML. Heme A of cytochrome c oxidase; structure and properties: comparisons with heme B, heme-C and heme-S and derivatives. J Biol Chem 250: 7602-7622, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 7602-7622
    • Caughey, W.S.1    Smythe, G.A.2    Okeeffe, D.H.3    Maskasky, J.E.4    Smith, M.L.5
  • 55
    • 0011062898 scopus 로고
    • Functional intermediates in reaction of cytochrome oxidase with oxygen
    • Chance B, Saronio C, and Leigh JS. Functional intermediates in reaction of cytochrome oxidase with oxygen. Proc Natl Acad Sci U S A 72: 1635-1640, 1975.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 1635-1640
    • Chance, B.1    Saronio, C.2    Leigh, J.S.3
  • 56
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex: Function in the context of structure
    • 1 complex: function in the context of structure. Annu Rev Physiol 66: 689-733, 2004.
    • (2004) Annu Rev Physiol , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 57
    • 0002036605 scopus 로고
    • Sur la decomposition de l'eau et des corps qu'elle tient en dissolution a l'aide de l'electricite galvanique
    • de Grotthuss CJT. Sur la decomposition de l'eau et des corps qu'elle tient en dissolution a l'aide de l'electricite galvanique. Ann Chim (Paris) LVIII: 54-74, 1806.
    • (1806) Ann Chim (Paris) , vol.58 , pp. 54-74
    • de Grotthuss, C.J.T.1
  • 59
    • 0018392155 scopus 로고
    • Lipid-impregnated filters as a tool for studying the electric current-generating proteins
    • Drachev LA, Kaulen AD, Semenov AY, Severina II, and Skulachev VP. Lipid-impregnated filters as a tool for studying the electric current-generating proteins. Anal Biochem 96: 250-262, 1979.
    • (1979) Anal Biochem , vol.96 , pp. 250-262
    • Drachev, L.A.1    Kaulen, A.D.2    Semenov, A.Y.3    Severina II4    Skulachev, V.P.5
  • 60
    • 0028955899 scopus 로고
    • Fast reactions of cytochrome oxidase
    • Einarsdottir O. Fast reactions of cytochrome oxidase. Biochim Biophys Acta 1229: 129-147, 1995.
    • (1995) Biochim Biophys Acta , vol.1229 , pp. 129-147
    • Einarsdottir, O.1
  • 61
    • 0021871425 scopus 로고
    • Bovine heart cytochrome c oxidase preparations contain high affinity binding sites for magnesium as well as for zinc, copper, and heme iron
    • Einarsdottir O, Caughey WS. Bovine heart cytochrome c oxidase preparations contain high affinity binding sites for magnesium as well as for zinc, copper, and heme iron. Biochem Biophys Res Commun 129: 840-847, 1985.
    • (1985) Biochem Biophys Res Commun , vol.129 , pp. 840-847
    • Einarsdottir, O.1    Caughey, W.S.2
  • 63
    • 0028964820 scopus 로고
    • Intramolecular electron transfer and conformational changes in cytochrome c oxidase
    • Einarsdottir O, Georgiadis KE, and Sucheta A. Intramolecular electron transfer and conformational changes in cytochrome c oxidase. Biochemistry 34: 496-508, 1995.
    • (1995) Biochemistry , vol.34 , pp. 496-508
    • Einarsdottir, O.1    Georgiadis, K.E.2    Sucheta, A.3
  • 64
    • 0033539479 scopus 로고    scopus 로고
    • Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase
    • Fabian M, Wong WW, Gennis RB, and Palmer G. Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase. Proc Natl Acad Sci U S A 96: 13114-13117, 1999.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13114-13117
    • Fabian, M.1    Wong, W.W.2    Gennis, R.B.3    Palmer, G.4
  • 66
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxen K, Gilderson G, Ädelroth P, and Brzezinski P. A mechanistic principle for proton pumping by cytochrome c oxidase. Nature 437: 286-289, 2005.
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxen, K.1    Gilderson, G.2    Ädelroth, P.3    Brzezinski, P.4
  • 68
    • 28844473846 scopus 로고    scopus 로고
    • Opinion: Radical medicine: treating ageing to cure disease
    • Finkel T. Opinion: Radical medicine: treating ageing to cure disease. Nat Rev Mol Cell Biol 6: 971-976, 2005.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 971-976
    • Finkel, T.1
  • 69
    • 0019887629 scopus 로고
    • Covalent complex between yeast cytochrome c and beef heart cytochrome c oxidase which is active in electron transfer
    • Fuller SD, Darley-Usmar VM, and Capaldi RA. Covalent complex between yeast cytochrome c and beef heart cytochrome c oxidase which is active in electron transfer. Biochemistry 20: 7046-7053, 1981.
    • (1981) Biochemistry , vol.20 , pp. 7046-7053
    • Fuller, S.D.1    Darley-Usmar, V.M.2    Capaldi, R.A.3
  • 71
    • 0022974929 scopus 로고
    • The proton-pumping site of cytochrome c oxidase: A model of its structure and mechanism
    • Gelles J, Blair DF, and Chan SI. The proton-pumping site of cytochrome c oxidase: a model of its structure and mechanism. Biochim Biophys Acta 853: 205-236, 1986.
    • (1986) Biochim Biophys Acta , vol.853 , pp. 205-236
    • Gelles, J.1    Blair, D.F.2    Chan, S.I.3
  • 72
    • 0028819233 scopus 로고
    • Design of a ruthenium-cytochrome c derivative to measure electron transfer to the initial acceptor in cytochrome c oxidase
    • Geren LM, Beasley JR, Fine BR, Saunders AJ, Hibdon S, Pielak GJ, Durham B, and Millett F. Design of a ruthenium-cytochrome c derivative to measure electron transfer to the initial acceptor in cytochrome c oxidase. J Biol Chem 270: 2466-2472, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 2466-2472
    • Geren, L.M.1    Beasley, J.R.2    Fine, B.R.3    Saunders, A.J.4    Hibdon, S.5    Pielak, G.J.6    Durham, B.7    Millett, F.8
  • 73
    • 0000825077 scopus 로고
    • Reactions of cytochrome oxidase with oxygen and carbon monoxide
    • Gibson QH and Greenwood C. Reactions of cytochrome oxidase with oxygen and carbon monoxide. Biochem J 86: 541-545, 1963.
    • (1963) Biochem J , vol.86 , pp. 541-545
    • Gibson, Q.H.1    Greenwood, C.2
  • 74
    • 17644402574 scopus 로고
    • The spectra and some properties of cytochrome oxidase components
    • Gibson QH and Greenwood C. The spectra and some properties of cytochrome oxidase components. J Biol Chem 239: 586-590, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 586-590
    • Gibson, Q.H.1    Greenwood, C.2
  • 75
    • 0842334759 scopus 로고    scopus 로고
    • Oxygen conformance of cellular respiration: A perspective of mitochondrial physiology
    • Gnaiger E. Oxygen conformance of cellular respiration: a perspective of mitochondrial physiology. Adv Exp Med Biol 543: 39-55, 2003.
    • (2003) Adv Exp Med Biol , vol.543 , pp. 39-55
    • Gnaiger, E.1
  • 76
    • 33646355978 scopus 로고    scopus 로고
    • Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy
    • Gorbikova EA, Vuorilehto K, Wikström M, and Verkhovsky MI. Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy. Biochemistry 45: 5641-5649, 2006.
    • (2006) Biochemistry , vol.45 , pp. 5641-5649
    • Gorbikova, E.A.1    Vuorilehto, K.2    Wikström, M.3    Verkhovsky, M.I.4
  • 77
    • 0029895160 scopus 로고    scopus 로고
    • Electron transfer in proteins
    • Gray HB and Winkler JR. Electron transfer in proteins. Annu Rev Biochem 65: 537-561, 1996.
    • (1996) Annu Rev Biochem , vol.65 , pp. 537-561
    • Gray, H.B.1    Winkler, J.R.2
  • 78
    • 0022542231 scopus 로고
    • 558 component of the cytochrome d complex from Escherichia coli
    • 558 component of the cytochrome d complex from Escherichia coli. Biochemistry 25: 2309-2314, 1986.
    • (1986) Biochemistry , vol.25 , pp. 2309-2314
    • Green, G.N.1    Lorence, R.M.2    Gennis, R.B.3
  • 79
    • 0028219639 scopus 로고
    • Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site
    • Hallen S, Brzezinski P, and Malmström BG. 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.
    • (1994) Biochemistry , vol.33 , pp. 1467-1472
    • Hallen, S.1    Brzezinski, P.2    Malmström, B.G.3
  • 80
    • 0024845389 scopus 로고
    • Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase
    • Haltia T, Finel M, Harms N, Nakari T, Raitio M, Wikström M, and Saraste M. Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase. EMBO J 8: 3571-3579, 1989.
    • (1989) EMBO J , vol.8 , pp. 3571-3579
    • Haltia, T.1    Finel, M.2    Harms, N.3    Nakari, T.4    Raitio, M.5    Wikström, M.6    Saraste, M.7
  • 81
    • 0025879301 scopus 로고
    • Subunit III of cytochrome c oxidase is not involved in proton translocation: A site-directed mutagenesis study
    • Haltia T, Saraste M, and Wikström M. Subunit III of cytochrome c oxidase is not involved in proton translocation: a site-directed mutagenesis study. EMBO J 10: 2015-2021, 1991.
    • (1991) EMBO J , vol.10 , pp. 2015-2021
    • Haltia, T.1    Saraste, M.2    Wikström, M.3
  • 82
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans
    • Haltia T, Semo N, Arrondo JL, Goni FM, and Freire E. Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 33: 9731-9740, 1994.
    • (1994) Biochemistry , vol.33 , pp. 9731-9740
    • Haltia, T.1    Semo, N.2    Arrondo, J.L.3    Goni, F.M.4    Freire, E.5
  • 83
    • 0025096278 scopus 로고
    • Cytochrome c oxidase: Decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a
    • Han S, Ching YC, and Rousseau DL. Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a. Proc Natl Acad Sci U S A 87: 8408-8412, 1990.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 8408-8412
    • Han, S.1    Ching, Y.C.2    Rousseau, D.L.3
  • 84
    • 0025269442 scopus 로고
    • Primary intermediate in the reaction of oxygen with fully reduced cytochrome c oxidase
    • Han S, Ching YC, and Rousseau DL. Primary intermediate in the reaction of oxygen with fully reduced cytochrome c oxidase. Proc Natl Acad Sci U S A 87: 2491-2495, 1990.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 2491-2495
    • Han, S.1    Ching, Y.C.2    Rousseau, D.L.3
  • 85
    • 0033585083 scopus 로고    scopus 로고
    • The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction
    • Harrenga A and Michel H. The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction. J Biol Chem 274: 33296-33299, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 33296-33299
    • Harrenga, A.1    Michel, H.2
  • 86
    • 0026016270 scopus 로고
    • Ionic strength dependence of the kinetics of electron transfer from bovine mitochondrial cytochrome c to bovine cytochrome c oxidase
    • Hazzard JT, Rong SY, and Tollin G. Ionic strength dependence of the kinetics of electron transfer from bovine mitochondrial cytochrome c to bovine cytochrome c oxidase. Biochemistry 30: 213-222, 1991.
    • (1991) Biochemistry , vol.30 , pp. 213-222
    • Hazzard, J.T.1    Rong, S.Y.2    Tollin, G.3
  • 88
    • 0037133132 scopus 로고    scopus 로고
    • Proton and electron pathways in the bacterial nitric oxide reductase
    • Hendriks JH, Jasaitis A, Saraste M, and Verkhovsky MI. Proton and electron pathways in the bacterial nitric oxide reductase. Biochemistry 41: 2331-2340, 2002.
    • (2002) Biochemistry , vol.41 , pp. 2331-2340
    • Hendriks, J.H.1    Jasaitis, A.2    Saraste, M.3    Verkhovsky, M.I.4
  • 89
    • 0030874890 scopus 로고    scopus 로고
    • ADP-regulation of mitochondrial free radical production is different with complex I- or complex II-linked substrates: Implications for the exercise paradox and brain hypermetabolism
    • Herrero A and Barja G. ADP-regulation of mitochondrial free radical production is different with complex I- or complex II-linked substrates: implications for the exercise paradox and brain hypermetabolism. J Bioenerg Biomembr 29: 241-249, 1997.
    • (1997) J Bioenerg Biomembr , vol.29 , pp. 241-249
    • Herrero, A.1    Barja, G.2
  • 90
    • 0025861459 scopus 로고
    • The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen
    • Hill BC. The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen. J Biol Chem 266: 2219-2226, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 2219-2226
    • Hill, B.C.1
  • 91
    • 0027993918 scopus 로고
    • Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase with oxygen
    • Hill BC. Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase with oxygen. J Biol Chem 269: 2419-2425, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 2419-2425
    • Hill, B.C.1
  • 92
    • 0020984324 scopus 로고
    • 2) in the reaction of mixedvalence cytochrome c oxidase with oxygen at room temperature
    • 2) in the reaction of mixedvalence cytochrome c oxidase with oxygen at room temperature. Biochem J 215: 659-667, 1983.
    • (1983) Biochem J , vol.215 , pp. 659-667
    • Hill, B.C.1    Greenwood, C.2
  • 93
    • 0021763113 scopus 로고
    • The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature: Evidence for new pathways of electron transfer
    • Hill BC and Greenwood C. The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature: evidence for new pathways of electron transfer. Biochem J 218: 913-921, 1984.
    • (1984) Biochem J , vol.218 , pp. 913-921
    • Hill, B.C.1    Greenwood, C.2
  • 95
    • 23044477952 scopus 로고    scopus 로고
    • Organization of iron-sulfur clusters in respiratory complex I
    • Hinchliffe P and Sazanov LA. Organization of iron-sulfur clusters in respiratory complex I. Science 309: 771-774, 2005.
    • (2005) Science , vol.309 , pp. 771-774
    • Hinchliffe, P.1    Sazanov, L.A.2
  • 96
    • 0018370326 scopus 로고
    • Proton translocation by cytochrome c oxidase incorporated into phospholipid vesicles
    • Hinkle PC. Proton translocation by cytochrome c oxidase incorporated into phospholipid vesicles. Methods Enzymol 55: 748-751, 1979.
    • (1979) Methods Enzymol , vol.55 , pp. 748-751
    • Hinkle, P.C.1
  • 97
    • 21044445453 scopus 로고    scopus 로고
    • Energy transduction by respiratory complex I: An evaluation of current knowledge
    • Hirst J. Energy transduction by respiratory complex I: an evaluation of current knowledge. Biochem Soc Trans 33: 525-529, 2005.
    • (2005) Biochem Soc Trans , vol.33 , pp. 525-529
    • Hirst, J.1
  • 98
    • 0031973948 scopus 로고    scopus 로고
    • Oxygen and proton pathways in cytochrome c oxidase
    • Hofacker I and Schulten K. Oxygen and proton pathways in cytochrome c oxidase. Proteins 30: 100-107, 1998.
    • (1998) Proteins , vol.30 , pp. 100-107
    • Hofacker, I.1    Schulten, K.2
  • 99
    • 0007811437 scopus 로고
    • Cytochrome c oxidase components. I: Purification and properties
    • Horie S and Morrison M. Cytochrome c oxidase components. I: purification and properties. J Biol Chem 238: 1855-1860, 1963.
    • (1963) J Biol Chem , vol.238 , pp. 1855-1860
    • Horie, S.1    Morrison, M.2
  • 101
    • 0029010688 scopus 로고
    • Analysis of site-directed mutants locates a non-redox-active metal near the active site of cytochrome c oxidase of Rhodobacter sphaeroides
    • Hosler JP, Espe MP, Zhen Y, Babcock GT, and Ferguson-Miller S. Analysis of site-directed mutants locates a non-redox-active metal near the active site of cytochrome c oxidase of Rhodobacter sphaeroides. Biochemistry 34: 7586-7592, 1995.
    • (1995) Biochemistry , vol.34 , pp. 7586-7592
    • Hosler, J.P.1    Espe, M.P.2    Zhen, Y.3    Babcock, G.T.4    Ferguson-Miller, S.5
  • 105
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, and Michel H. Structure at 2.8 Å 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
  • 106
    • 33750036104 scopus 로고    scopus 로고
    • Spectral and kinetic equivalence of oxidized cytochrome c oxidase as isolated and "activated" by reoxidation
    • Jancura D, Berka V, Antalik M, Bagelova J, Gennis RB, Palmer G, and Fabian M. Spectral and kinetic equivalence of oxidized cytochrome c oxidase as isolated and "activated" by reoxidation. J Biol Chem 281: 30319-30325, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 30319-30325
    • Jancura, D.1    Berka, V.2    Antalik, M.3    Bagelova, J.4    Gennis, R.B.5    Palmer, G.6    Fabian, M.7
  • 107
    • 0035340281 scopus 로고    scopus 로고
    • Electron and proton transfer in the arginine-54-methionine mutant of cytochrome c oxidase from Paracoccus denitrificans
    • Jasaitis A, Backgren C, Morgan JE, Puustinen A, Verkhovsky MI, and Wikström M. Electron and proton transfer in the arginine-54-methionine mutant of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 40: 5269-5274, 2001.
    • (2001) Biochemistry , vol.40 , pp. 5269-5274
    • Jasaitis, A.1    Backgren, C.2    Morgan, J.E.3    Puustinen, A.4    Verkhovsky, M.I.5    Wikström, M.6
  • 108
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen
    • Jasaitis A, Verkhovsky MI, Morgan JE, Verkhovskaya ML, and Wikström M. Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen. Biochemistry 38: 2697-2706, 1999.
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Verkhovskaya, M.L.4    Wikström, M.5
  • 109
    • 0035795143 scopus 로고    scopus 로고
    • Fungal respiration: A fusion of standard and alternative components
    • Joseph-Horne T, Hollomon DW, and Wood PM. Fungal respiration: a fusion of standard and alternative components. Biochim Biophys Acta 1504: 179-195, 2001.
    • (2001) Biochim Biophys Acta , vol.1504 , pp. 179-195
    • Joseph-Horne, T.1    Hollomon, D.W.2    Wood, P.M.3
  • 110
    • 0343714594 scopus 로고    scopus 로고
    • Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase
    • Kadenbach B, Huttemann M, Arnold S, Lee I, and Bender E. Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase. Free Radic Biol Med 29: 211-221, 2000.
    • (2000) Free Radic Biol Med , vol.29 , pp. 211-221
    • Kadenbach, B.1    Huttemann, M.2    Arnold, S.3    Lee, I.4    Bender, E.5
  • 111
    • 0019891622 scopus 로고
    • On the function of multiple subunits of cytochrome c oxidase from higher eukaryotes
    • Kadenbach B and Merle P. On the function of multiple subunits of cytochrome c oxidase from higher eukaryotes. FEBS Lett 135: 1-11, 1981.
    • (1981) FEBS Lett , vol.135 , pp. 1-11
    • Kadenbach, B.1    Merle, P.2
  • 112
    • 7144257841 scopus 로고    scopus 로고
    • The role of electrostatic interactions for cytochrome c oxidase function
    • Kannt A, Lancaster CR, and Michel H. The role of electrostatic interactions for cytochrome c oxidase function. J Bioenerg Biomembr 30: 81-87, 1998.
    • (1998) J Bioenerg Biomembr , vol.30 , pp. 81-87
    • Kannt, A.1    Lancaster, C.R.2    Michel, H.3
  • 113
    • 0033621496 scopus 로고    scopus 로고
    • Mutation of Arg-54 strongly influences heme composition and rate and directionality of electron transfer in Paracoccus denitrificans cytochrome c oxidase
    • Kannt A, Pfitzner U, Ruitenberg M, Hellwig P, Ludwig B, Mäntele W, Fendler K, and Michel H. Mutation of Arg-54 strongly influences heme composition and rate and directionality of electron transfer in Paracoccus denitrificans cytochrome c oxidase. J Biol Chem 274: 37974-37981, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 37974-37981
    • Kannt, A.1    Pfitzner, U.2    Ruitenberg, M.3    Hellwig, P.4    Ludwig, B.5    Mäntele, W.6    Fendler, K.7    Michel, H.8
  • 114
    • 0000955795 scopus 로고
    • An EPR-detectable intermediate in the cytochrome oxidase-dioxygen reaction
    • Karlsson B, Aasa R, Vanngård T, and Malmström BG. An EPR-detectable intermediate in the cytochrome oxidase-dioxygen reaction. FEBS Lett 131: 186-188, 1981.
    • (1981) FEBS Lett , vol.131 , pp. 186-188
    • Karlsson, B.1    Aasa, R.2    Vanngård, T.3    Malmström, B.G.4
  • 115
    • 0019878506 scopus 로고
    • The identity of a new copper(II) electron paramagnetic resonance signal in cytochrome c oxidase
    • Karlsson B and Andreasson LE. The identity of a new copper(II) electron paramagnetic resonance signal in cytochrome c oxidase. Biochim Biophys Acta 635: 73-80, 1981.
    • (1981) Biochim Biophys Acta , vol.635 , pp. 73-80
    • Karlsson, B.1    Andreasson, L.E.2
  • 116
    • 0034727649 scopus 로고    scopus 로고
    • Formation of the "peroxy" intermediate in cytochrome c oxidase is associated with internal proton/hydrogen transfer
    • Karpefors M, Ädelroth P, Namslauer A, Zhen Y, and Brzezinski P. Formation of the "peroxy" intermediate in cytochrome c oxidase is associated with internal proton/hydrogen transfer. Biochemistry 39: 14664-14669, 2000.
    • (2000) Biochemistry , vol.39 , pp. 14664-14669
    • Karpefors, M.1    Ädelroth, P.2    Namslauer, A.3    Zhen, Y.4    Brzezinski, P.5
  • 117
    • 0001723423 scopus 로고
    • On cytochrome, a respiratory pigment common to animals, yeast, and higher plants
    • Keilin D. On cytochrome, a respiratory pigment common to animals, yeast, and higher plants. Proc R Soc Lond B Biol Sci 98: 312-339, 1925.
    • (1925) Proc R Soc Lond B Biol Sci , vol.98 , pp. 312-339
    • Keilin, D.1
  • 118
    • 0037510071 scopus 로고
    • Influence of carbon monoxide and light on indophenol oxidase of yeast cells
    • Keilin D. Influence of carbon monoxide and light on indophenol oxidase of yeast cells. Nature 119: 670-671, 1927.
    • (1927) Nature , vol.119 , pp. 670-671
    • Keilin, D.1
  • 119
    • 0027166085 scopus 로고
    • Two cysteines, two histidines, and one methionine are ligands of a binuclear purple copper center
    • Kelly M, Lappalainen P, Talbo G, Haltia T, van der OJ, and Saraste M. Two cysteines, two histidines, and one methionine are ligands of a binuclear purple copper center. J Biol Chem 268: 16781-16787, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 16781-16787
    • Kelly, M.1    Lappalainen, P.2    Talbo, G.3    Haltia, T.4    van der, O.J.5    Saraste, M.6
  • 120
    • 0025030204 scopus 로고
    • Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: Mutants deficient in the cytochrome d complex are unable to fix nitrogen in air
    • Kelly MJ, Poole RK, Yates MG, and Kennedy C. Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air. J Bacteriol 172: 6010-6019, 1990.
    • (1990) J Bacteriol , vol.172 , pp. 6010-6019
    • Kelly, M.J.1    Poole, R.K.2    Yates, M.G.3    Kennedy, C.4
  • 122
    • 0024405649 scopus 로고
    • Electron transfer process in cytochrome oxidase after pulse radiolysis
    • Kobayashi K, Une H, and Hayashi K. Electron transfer process in cytochrome oxidase after pulse radiolysis. J Biol Chem 264: 7976-7980, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 7976-7980
    • Kobayashi, K.1    Une, H.2    Hayashi, K.3
  • 123
    • 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
    • Konstantinov AA, Siletsky S, Mitchell D, Kaulen A, and Gennis RB. 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.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 124
    • 0018185852 scopus 로고
    • Proton-translocating cytochrome c oxidase in artificial phospholipid vesicles
    • Krab K and Wikström M. Proton-translocating cytochrome c oxidase in artificial phospholipid vesicles. Biochim Biophys Acta 504: 200-214, 1978.
    • (1978) Biochim Biophys Acta , vol.504 , pp. 200-214
    • Krab, K.1    Wikström, M.2
  • 126
    • 0026526374 scopus 로고
    • Isolation and characterization of COX12, the nuclear gene for a previously unrecognized subunit of Saccharomyces cerevisiae cytochrome c oxidase
    • LaMarche AE, Abate MI, Chan SH, and Trumpower BL. Isolation and characterization of COX12, the nuclear gene for a previously unrecognized subunit of Saccharomyces cerevisiae cytochrome c oxidase. J Biol Chem 267: 22473-22480, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 22473-22480
    • LaMarche, A.E.1    Abate, M.I.2    Chan, S.H.3    Trumpower, B.L.4
  • 127
    • 2942556920 scopus 로고    scopus 로고
    • X-ray diffraction of bacteriorhodopsin photocycle intermediates
    • Lanyi JK. X-ray diffraction of bacteriorhodopsin photocycle intermediates. Mol Membr Biol 21: 143-150, 2004.
    • (2004) Mol Membr Biol , vol.21 , pp. 143-150
    • Lanyi, J.K.1
  • 131
    • 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
    • Lee HM, Das TK, Rousseau DL, Mills D, Ferguson-Miller S, and Gennis RB. 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.
    • (2000) Biochemistry , vol.39 , pp. 2989-2996
    • Lee, H.M.1    Das, T.K.2    Rousseau, D.L.3    Mills, D.4    Ferguson-Miller, S.5    Gennis, R.B.6
  • 132
    • 36949071287 scopus 로고    scopus 로고
    • Lemberg R. Action of alkali on cytochrome oxidase. Nature 193: 373-000, 1962.
    • Lemberg R. Action of alkali on cytochrome oxidase. Nature 193: 373-000, 1962.
  • 135
  • 136
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus RA and Sutin N. Electron transfers in chemistry and biology. Biochim Biophys Acta 811: 265-322, 1985.
    • (1985) Biochim Biophys Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 137
    • 0034654622 scopus 로고    scopus 로고
    • Insights into the functional role of the tyrosine-histidine linkage in cytochrome c oxidase
    • McCauley KM, Vrtis JM, Dupont J, and van der Donk WA. Insights into the functional role of the tyrosine-histidine linkage in cytochrome c oxidase. J Am Chem Soc 122: 2403-2404, 2000.
    • (2000) J Am Chem Soc , vol.122 , pp. 2403-2404
    • McCauley, K.M.1    Vrtis, J.M.2    Dupont, J.3    van der Donk, W.A.4
  • 138
    • 0032573072 scopus 로고    scopus 로고
    • The mechanism of proton pumping by cytochrome c oxidase
    • Michel H. The mechanism of proton pumping by cytochrome c oxidase. Proc Natl Acad Sci U S A 95: 12819-12824, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12819-12824
    • Michel, H.1
  • 139
    • 0022383731 scopus 로고
    • The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli
    • Miller MJ and Gennis RB. The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli. J Biol Chem 260: 14003-14008, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 14003-14008
    • Miller, M.J.1    Gennis, R.B.2
  • 140
    • 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
  • 141
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P. Possible molecular mechanisms of the protonmotive function of cytochrome systems. J Theor Biol 62: 327-367, 1976.
    • (1976) J Theor Biol , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 142
    • 0024393891 scopus 로고
    • Possible protonmotive osmochemistry in cytochrome oxidase
    • Mitchell P. Possible protonmotive osmochemistry in cytochrome oxidase. Ann N Y Acad Sci 550: 185-198, 1988.
    • (1988) Ann N Y Acad Sci , vol.550 , pp. 185-198
    • Mitchell, P.1
  • 143
    • 0026034054 scopus 로고
    • The assignment of the 655 nm spectral band of cytochrome oxidase
    • Mitchell R, Mitchell P, and Rich PR. The assignment of the 655 nm spectral band of cytochrome oxidase. FEBS Lett 280: 321-324, 1991.
    • (1991) FEBS Lett , vol.280 , pp. 321-324
    • Mitchell, R.1    Mitchell, P.2    Rich, P.R.3
  • 144
    • 0028241769 scopus 로고
    • Proton uptake by cytochrome c oxidase on reduction and on ligand binding
    • Mitchell R and Rich PR. Proton uptake by cytochrome c oxidase on reduction and on ligand binding. Biochim Biophys Acta 1186: 19-26, 1994.
    • (1994) Biochim Biophys Acta , vol.1186 , pp. 19-26
    • Mitchell, R.1    Rich, P.R.2
  • 145
    • 0025993819 scopus 로고
    • Single electron reduction of "slow" and "fast" cytochrome-c oxidase
    • Moody AJ, Brandt U, and Rich PR. Single electron reduction of "slow" and "fast" cytochrome-c oxidase. FEBS Lett 293: 101-105, 1991.
    • (1991) FEBS Lett , vol.293 , pp. 101-105
    • Moody, A.J.1    Brandt, U.2    Rich, P.R.3
  • 146
    • 0025772795 scopus 로고
    • Characterisation of "fast" and "slow" forms of bovine heart cytochrome-c oxidase
    • Moody AJ, Cooper CE, and Rich PR. Characterisation of "fast" and "slow" forms of bovine heart cytochrome-c oxidase. Biochim Biophys Acta 1059: 189-207, 1991.
    • (1991) Biochim Biophys Acta , vol.1059 , pp. 189-207
    • Moody, A.J.1    Cooper, C.E.2    Rich, P.R.3
  • 147
    • 0025125898 scopus 로고
    • The effect of pH on redox titrations of haem a in cyanide-liganded cytochrome-c oxidase: Experimental and modelling studies
    • Moody AJ and Rich PR. The effect of pH on redox titrations of haem a in cyanide-liganded cytochrome-c oxidase: experimental and modelling studies. Biochim Biophys Acta 1015: 205-215, 1990.
    • (1990) Biochim Biophys Acta , vol.1015 , pp. 205-215
    • Moody, A.J.1    Rich, P.R.2
  • 148
    • 0024448807 scopus 로고
    • Electron transfer between cytochrome a and copper A in cytochrome c oxidase: A perturbed equilibrium study
    • Morgan JE, Li PM, Jang DJ, el Sayed MA, and Chan SI. Electron transfer between cytochrome a and copper A in cytochrome c oxidase: a perturbed equilibrium study. Biochemistry 28: 6975-6983, 1989.
    • (1989) Biochemistry , vol.28 , pp. 6975-6983
    • Morgan, J.E.1    Li, P.M.2    Jang, D.J.3    el Sayed, M.A.4    Chan, S.I.5
  • 150
    • 0028607633 scopus 로고
    • The histidine cycle: A new model for proton translocation in the respiratory hemecopper oxidases
    • Morgan JE, Verkhovsky MI, and Wikström M. The histidine cycle: a new model for proton translocation in the respiratory hemecopper oxidases. J Bioenerg Biomembr 26: 599-608, 1994.
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 599-608
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 151
    • 0029775911 scopus 로고    scopus 로고
    • Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase
    • Morgan JE, Verkhovsky MI, and Wikström M. Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase. Biochemistry 35: 12235-12240, 1996.
    • (1996) Biochemistry , vol.35 , pp. 12235-12240
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 154
    • 0345613372 scopus 로고
    • Molecular mechanisms for proton transport in membranes
    • Nagle JF and Morowitz HJ. Molecular mechanisms for proton transport in membranes. Proc Natl Acad Sci U S A 75: 298-302, 1978.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 298-302
    • Nagle, J.F.1    Morowitz, H.J.2
  • 155
    • 0026723615 scopus 로고
    • Photoinduced electron transfer from tris(2,2′-bipyridyl) ruthenium to cytochrome c oxidase
    • Nilsson T. Photoinduced electron transfer from tris(2,2′-bipyridyl) ruthenium to cytochrome c oxidase. Proc Natl Acad Sci U S A 89: 6497-6501, 1992.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6497-6501
    • Nilsson, T.1
  • 157
    • 0024408677 scopus 로고
    • The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen
    • Oliveberg M, Brzezinski P, and Malmström BG. The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen. Biochim Biophys Acta 977: 322-328, 1989.
    • (1989) Biochim Biophys Acta , vol.977 , pp. 322-328
    • Oliveberg, M.1    Brzezinski, P.2    Malmström, B.G.3
  • 158
    • 0025981255 scopus 로고
    • Uptake and release of protons during the reaction between cytochrome c oxidase and molecular oxygen: A flow-flash investigation
    • Oliveberg M, Hallen S, and Nilsson T. Uptake and release of protons during the reaction between cytochrome c oxidase and molecular oxygen: a flow-flash investigation. Biochemistry 30: 436-440, 1991.
    • (1991) Biochemistry , vol.30 , pp. 436-440
    • Oliveberg, M.1    Hallen, S.2    Nilsson, T.3
  • 159
    • 0025841838 scopus 로고
    • Internal electron transfer in cytochrome c oxidase: Evidence for a rapid equilibrium between cytochrome a and the bimetallic site
    • Oliveberg M, Malmström BG. Internal electron transfer in cytochrome c oxidase: evidence for a rapid equilibrium between cytochrome a and the bimetallic site. Biochemistry 30: 7053-7057, 1991.
    • (1991) Biochemistry , vol.30 , pp. 7053-7057
    • Oliveberg, M.1    Malmström, B.G.2
  • 160
    • 0026778190 scopus 로고
    • Reaction of dioxygen with cytochrome c oxidase reduced to different degrees: Indications of a transient dioxygen complex with copper-B
    • Oliveberg M, Malmström BG. Reaction of dioxygen with cytochrome c oxidase reduced to different degrees: indications of a transient dioxygen complex with copper-B. Biochemistry 31: 3560-3563, 1992.
    • (1992) Biochemistry , vol.31 , pp. 3560-3563
    • Oliveberg, M.1    Malmström, B.G.2
  • 161
    • 0024196873 scopus 로고
    • Intermediates in the reaction of reduced cytochrome oxidase with dioxygen
    • Orii Y. Intermediates in the reaction of reduced cytochrome oxidase with dioxygen. Ann N Y Acad Sci 550: 105-117, 1988.
    • (1988) Ann N Y Acad Sci , vol.550 , pp. 105-117
    • Orii, Y.1
  • 162
    • 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
    • Ostermeier C, Harrenga A, Ermler U, and Michel H. 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.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 163
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page CC, Moser CC, Chen X, and Dutton PL. 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
  • 164
    • 0032515180 scopus 로고    scopus 로고
    • A cooperative model for protonmotive heme-copper oxidases: The role of heme a in the proton pump of cytochrome c oxidase
    • Papa S, Capitanio N, and Villani G. A cooperative model for protonmotive heme-copper oxidases: the role of heme a in the proton pump of cytochrome c oxidase. FEBS Lett 439: 1-8, 1998.
    • (1998) FEBS Lett , vol.439 , pp. 1-8
    • Papa, S.1    Capitanio, N.2    Villani, G.3
  • 165
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron-transfer partners, cytochrome c peroxidase and cytochrome c
    • Pelletier H and Kraut J. Crystal structure of a complex between electron-transfer partners, cytochrome c peroxidase and cytochrome c. Science 258: 1748-1755, 1992.
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 169
    • 9244257845 scopus 로고    scopus 로고
    • Electron transfer between hemes in mammalian cytochrome c oxidase
    • Pilet E, Jasaitis A, Liebl U, and Vos MH. Electron transfer between hemes in mammalian cytochrome c oxidase. Proc Natl Acad Sci U S A 101: 16198-16203, 2004.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16198-16203
    • Pilet, E.1    Jasaitis, A.2    Liebl, U.3    Vos, M.H.4
  • 170
    • 0021104863 scopus 로고
    • Bacterial cytochrome oxidases: A structurally and functionally diverse group of electron-transfer proteins
    • Poole RK. Bacterial cytochrome oxidases: a structurally and functionally diverse group of electron-transfer proteins. Biochim Biophys Acta 726: 205-243, 1983.
    • (1983) Biochim Biophys Acta , vol.726 , pp. 205-243
    • Poole, R.K.1
  • 171
    • 2442616154 scopus 로고    scopus 로고
    • Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating
    • Popovic DM and Stuchebrukhov AA. Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: coulomb pump model with kinetic gating. FEBS Lett 566: 126-130, 2004.
    • (2004) FEBS Lett , vol.566 , pp. 126-130
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 172
    • 0032493345 scopus 로고    scopus 로고
    • Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase
    • Proshlyakov DA, Pressler MA, and Babcock GT. Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. Proc Natl Acad Sci U S A 95: 8020-8025, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8020-8025
    • Proshlyakov, D.A.1    Pressler, M.A.2    Babcock, G.T.3
  • 175
    • 0024962043 scopus 로고
    • Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli
    • Puustinen A, Finel M, Virkki M, and Wikström M. Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli. FEBS Lett 249: 163-167, 1989.
    • (1989) FEBS Lett , vol.249 , pp. 163-167
    • Puustinen, A.1    Finel, M.2    Virkki, M.3    Wikström, M.4
  • 176
    • 0033524476 scopus 로고    scopus 로고
    • Proton exit from the heme-copper oxidase of Escherichia coli
    • Puustinen A and Wikström M. Proton exit from the heme-copper oxidase of Escherichia coli. Proc Natl Acad Sci U S A 96: 35-37, 1999.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 35-37
    • Puustinen, A.1    Wikström, M.2
  • 177
    • 33750807024 scopus 로고    scopus 로고
    • Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
    • Qin L, Hiser C, Mulichak A, Garavito RM, and Ferguson-Miller S. 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: 16117-16122, 2006.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2    Mulichak, A.3    Garavito, R.M.4    Ferguson-Miller, S.5
  • 178
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S and Robinson BH. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem Sci 25: 502-508, 2000.
    • (2000) Trends Biochem Sci , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 179
    • 0000673426 scopus 로고
    • Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus denitrificans
    • Raitio M, Jalli T, and Saraste M. Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus denitrificans. EMBO J 6: 2825-2833, 1987.
    • (1987) EMBO J , vol.6 , pp. 2825-2833
    • Raitio, M.1    Jalli, T.2    Saraste, M.3
  • 182
    • 29244472486 scopus 로고    scopus 로고
    • An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochrome c oxidase from Paracoccus denitrificans
    • Ribacka C, Verkhovsky MI, Belevich I, Bloch DA, Puustinen A, and Wikström M. An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 44: 16502-16512, 2005.
    • (2005) Biochemistry , vol.44 , pp. 16502-16512
    • Ribacka, C.1    Verkhovsky, M.I.2    Belevich, I.3    Bloch, D.A.4    Puustinen, A.5    Wikström, M.6
  • 183
    • 0017858515 scopus 로고
    • Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli
    • Rice CW and Hempfling WP. Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli. J Bacteriol 134: 115-124, 1978.
    • (1978) J Bacteriol , vol.134 , pp. 115-124
    • Rice, C.W.1    Hempfling, W.P.2
  • 184
  • 185
    • 0019332553 scopus 로고
    • 1: Differential acetylation of lysyl residues in free and complexed cytochrome c
    • 1: differential acetylation of lysyl residues in free and complexed cytochrome c. J Biol Chem 255: 4732-4739, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 4732-4739
    • Rieder, R.1    Bosshard, H.R.2
  • 186
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins
    • Rigaud JL, Pitard B, and Levy D. Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins. Biochim Biophys Acta 1231: 223-246, 1995.
    • (1995) Biochim Biophys Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 190
    • 0034732967 scopus 로고    scopus 로고
    • 2 and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans
    • 2 and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 39: 6365-6372, 2000.
    • (2000) Biochemistry , vol.39 , pp. 6365-6372
    • Riistama, S.1    Puustinen, A.2    Verkhovsky, M.I.3    Morgan, J.E.4    Wikström, M.5
  • 193
    • 0037007627 scopus 로고    scopus 로고
    • Reduction of cytochrome c oxidase by a second electron leads to proton translocation
    • Ruitenberg M, Kannt A, Bamberg E, Fendler K, and Michel H. Reduction of cytochrome c oxidase by a second electron leads to proton translocation. Nature 417: 99-102, 2002.
    • (2002) Nature , vol.417 , pp. 99-102
    • Ruitenberg, M.1    Kannt, A.2    Bamberg, E.3    Fendler, K.4    Michel, H.5
  • 194
    • 0034712938 scopus 로고    scopus 로고
    • Single-electron reduction of the oxidized state is coupled to proton uptake via the K pathway in Paracoccus denitrificans cytochrome c oxidase
    • Ruitenberg M, Kannt A, Bamberg E, Ludwig B, Michel H, and Fendler K. Single-electron reduction of the oxidized state is coupled to proton uptake via the K pathway in Paracoccus denitrificans cytochrome c oxidase. Proc Natl Acad Sci U S A 97: 4632-4636, 2000.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 4632-4636
    • Ruitenberg, M.1    Kannt, A.2    Bamberg, E.3    Ludwig, B.4    Michel, H.5    Fendler, K.6
  • 195
    • 0027442655 scopus 로고
    • In vitro heme O synthesis by the cyoE gene product from Escherichia coli
    • Saiki K, Mogi T, Ogura K, and Anraku Y. In vitro heme O synthesis by the cyoE gene product from Escherichia coli. J Biol Chem 268: 26041-26044, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 26041-26044
    • Saiki, K.1    Mogi, T.2    Ogura, K.3    Anraku, Y.4
  • 196
    • 4143060405 scopus 로고    scopus 로고
    • A single-amino-acid lid renders a gas-tight compartment within a membrane-bound transporter
    • Salomonsson L, Lee A, Gennis RB, and Brzezinski P. A single-amino-acid lid renders a gas-tight compartment within a membrane-bound transporter. Proc Natl Acad Sci U S A 101: 11617-11621, 2004.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 11617-11621
    • Salomonsson, L.1    Lee, A.2    Gennis, R.B.3    Brzezinski, P.4
  • 197
    • 0025640889 scopus 로고
    • Structural features of cytochrome oxidase
    • Saraste M. Structural features of cytochrome oxidase. Q Rev Biophys 23: 331-366, 1990.
    • (1990) Q Rev Biophys , vol.23 , pp. 331-366
    • Saraste, M.1
  • 198
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • Saraste M. Oxidative phosphorylation at the fin de siecle. Science 283: 1488-1493, 1999.
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 199
    • 0346103674 scopus 로고    scopus 로고
    • A discrete water exit pathway in the membrane protein cytochrome c oxidase
    • Schmidt B, McCracken J, and Ferguson-Miller S. A discrete water exit pathway in the membrane protein cytochrome c oxidase. Proc Natl Acad Sci U S A 100: 15539-15542, 2003.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 15539-15542
    • Schmidt, B.1    McCracken, J.2    Ferguson-Miller, S.3
  • 200
    • 0019361833 scopus 로고
    • Copper and manganese electron spin resonance studies of cytochrome c oxidase from Paracoccus denitrificans
    • Seelig A, Ludwig B, Seelig J, and Schatz G. Copper and manganese electron spin resonance studies of cytochrome c oxidase from Paracoccus denitrificans. Biochim Biophys Acta 636: 162-167, 1981.
    • (1981) Biochim Biophys Acta , vol.636 , pp. 162-167
    • Seelig, A.1    Ludwig, B.2    Seelig, J.3    Schatz, G.4
  • 201
    • 34347227058 scopus 로고    scopus 로고
    • Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1
    • Semenza GL. Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1. Biochem J 405: 1-9, 2007.
    • (2007) Biochem J , vol.405 , pp. 1-9
    • Semenza, G.L.1
  • 202
    • 0026583053 scopus 로고
    • 3-type cytochrome c oxidase of Rhodobacter sphaeroides
    • 3-type cytochrome c oxidase of Rhodobacter sphaeroides. Mol Microbiol 6: 635-642, 1992.
    • (1992) Mol Microbiol , vol.6 , pp. 635-642
    • Shapleigh, J.P.1    Gennis, R.B.2
  • 204
    • 0018196485 scopus 로고
    • 3 component of cytochrome c oxidase to substrate and ligand addition
    • 3 component of cytochrome c oxidase to substrate and ligand addition. Biochim Biophys Acta 504: 187-199, 1978.
    • (1978) Biochim Biophys Acta , vol.504 , pp. 187-199
    • Shaw, R.W.1    Hansen, R.E.2    Beinert, H.3
  • 206
    • 0142091718 scopus 로고    scopus 로고
    • Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase
    • Siegbahn PEM, Blomberg MRA, and Blomberg ML. Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase. J Phys Chem B 107: 10946-10955, 2003.
    • (2003) J Phys Chem B , vol.107 , pp. 10946-10955
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2    Blomberg, M.L.3
  • 207
    • 10644252589 scopus 로고    scopus 로고
    • Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase
    • Siletsky SA, Pawate AS, Weiss K, Gennis RB, and Konstantinov AA. Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase. J Biol Chem 279: 52558-52565, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 52558-52565
    • Siletsky, S.A.1    Pawate, A.S.2    Weiss, K.3    Gennis, R.B.4    Konstantinov, A.A.5
  • 208
    • 0038269101 scopus 로고    scopus 로고
    • Keilin, cytochrome, and the respiratory chain
    • Slater EC. Keilin, cytochrome, and the respiratory chain. J Biol Chem 278: 16455-16461, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 16455-16461
    • Slater, E.C.1
  • 209
    • 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
    • Smirnova IA, Ädelroth P, Gennis RB, and Brzezinski P. 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.
    • (1999) Biochemistry , vol.38 , pp. 6826-6833
    • Smirnova, I.A.1    Ädelroth, P.2    Gennis, R.B.3    Brzezinski, P.4
  • 210
    • 0020067210 scopus 로고
    • The cytochrome c oxidase of Paracoccus denitrificans pumps protons in a reconstituted system
    • Solioz M, Carafoli E, and Ludwig B. The cytochrome c oxidase of Paracoccus denitrificans pumps protons in a reconstituted system. J Biol Chem 257: 1579-1582, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 1579-1582
    • Solioz, M.1    Carafoli, E.2    Ludwig, B.3
  • 212
    • 0023656242 scopus 로고
    • Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA sequence, gene expression and the protein
    • Steinrucke P, Steffens GC, Panskus G, Buse G, and Ludwig B. Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA sequence, gene expression and the protein. Eur J Biochem 167: 431-439, 1987.
    • (1987) Eur J Biochem , vol.167 , pp. 431-439
    • Steinrucke, P.1    Steffens, G.C.2    Panskus, G.3    Buse, G.4    Ludwig, B.5
  • 214
    • 0032558999 scopus 로고    scopus 로고
    • Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen
    • Sucheta A, Szundi I, and Einarsdottir O. Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen. Biochemistry 37: 17905-17914, 1998.
    • (1998) Biochemistry , vol.37 , pp. 17905-17914
    • Sucheta, A.1    Szundi, I.2    Einarsdottir, O.3
  • 215
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • Svensson-Ek M, Abramson J, Larsson G, Tornroth S, Brzezinski P, and Iwata S. 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.
    • (2002) J Mol Biol , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 218
    • 0027380681 scopus 로고
    • Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center
    • Thomas JW, Lemieux LJ, Alben JO, and Gennis RB. Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center. Biochemistry 32: 11173-11180, 1993.
    • (1993) Biochemistry , vol.32 , pp. 11173-11180
    • Thomas, J.W.1    Lemieux, L.J.2    Alben, J.O.3    Gennis, R.B.4
  • 219
    • 0027491552 scopus 로고
    • Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity
    • Thomas JW, Puustinen A, Alben JO, Gennis RB, and Wikström M. Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity. Biochemistry 32: 10923-10928, 1993.
    • (1993) Biochemistry , vol.32 , pp. 10923-10928
    • Thomas, J.W.1    Puustinen, A.2    Alben, J.O.3    Gennis, R.B.4    Wikström, M.5
  • 223
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens JF, Alexandre A, and Lehninger AL. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch Biochem Biophys 237: 408-414, 1985.
    • (1985) Arch Biochem Biophys , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 224
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens JF and Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J 191: 421-427, 1980.
    • (1980) Biochem J , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 225
    • 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 and Wilson LJ. 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, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 8065-8071
    • Tweedle, M.F.1    Wilson, L.J.2
  • 227
    • 0014681476 scopus 로고
    • Studies of the heme components of cytochrome c oxidase by EPR spectroscopy
    • Van Gelder BF and Beinert H. Studies of the heme components of cytochrome c oxidase by EPR spectroscopy. Biochim Biophys Acta 189: 1-24, 1969.
    • (1969) Biochim Biophys Acta , vol.189 , pp. 1-24
    • Van Gelder, B.F.1    Beinert, H.2
  • 228
    • 0013889222 scopus 로고
    • 3 in cytochrome c oxidase
    • 3 in cytochrome c oxidase. Biochemistry 5: 838-848, 1966.
    • (1966) Biochemistry , vol.5 , pp. 838-848
    • Vanneste, W.H.1
  • 229
    • 0025195185 scopus 로고
    • IV = O) vibration from a ferryl-oxo intermediate in the cytochrome oxidase/dioxygen reaction
    • IV = O) vibration from a ferryl-oxo intermediate in the cytochrome oxidase/dioxygen reaction. Biochemistry 29: 7357-7362, 1990.
    • (1990) Biochemistry , vol.29 , pp. 7357-7362
    • Varotsis, C.1    Babcock, G.T.2
  • 232
    • 0026755167 scopus 로고
    • pH dependence of proton translocation by Escherichia coli
    • Verkhovskaya M, Verkhovsky M, and Wikström M. pH dependence of proton translocation by Escherichia coli. J Biol Chem 267: 14559-14562, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 14559-14562
    • Verkhovskaya, M.1    Verkhovsky, M.2    Wikström, M.3
  • 234
    • 33745602474 scopus 로고    scopus 로고
    • Elementary steps of proton translocation in the catalytic cycle of cytochrome oxidase
    • Verkhovsky MI, Belevich I, Bloch DA, and Wikström M. Elementary steps of proton translocation in the catalytic cycle of cytochrome oxidase. Biochim Biophys Acta 1757: 401-407, 2006.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 401-407
    • Verkhovsky, M.I.1    Belevich, I.2    Bloch, D.A.3    Wikström, M.4
  • 236
    • 0035519279 scopus 로고    scopus 로고
    • Ultrafast haem-haem electron transfer in cytochrome c oxidase
    • Verkhovsky MI, Jasaitis A, and Wikström M. Ultrafast haem-haem electron transfer in cytochrome c oxidase. Biochim Biophys Acta 1506: 143-146, 2001.
    • (2001) Biochim Biophys Acta , vol.1506 , pp. 143-146
    • Verkhovsky, M.I.1    Jasaitis, A.2    Wikström, M.3
  • 240
    • 0026496717 scopus 로고
    • Intramolecular electron transfer in cytochrome c oxidase: A cascade of equilibria
    • Verkhovsky MI, Morgan JE, and Wikström M. Intramolecular electron transfer in cytochrome c oxidase: a cascade of equilibria. Biochemistry 31: 11860-11863, 1992.
    • (1992) Biochemistry , vol.31 , pp. 11860-11863
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 241
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • Verkhovsky MI, Morgan JE, and Wikström M. Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase. Biochemistry 33: 3079-3086, 1994.
    • (1994) Biochemistry , vol.33 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 242
    • 0029036305 scopus 로고
    • Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons
    • Verkhovsky MI, Morgan JE, and Wikström M. Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: a role for protons. Biochemistry 34: 7483-7491, 1995.
    • (1995) Biochemistry , vol.34 , pp. 7483-7491
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 243
    • 0029926483 scopus 로고    scopus 로고
    • Redox transitions between oxygen intermediates in cytochrome-c oxidase
    • Verkhovsky MI, Morgan JE, and Wikström M. Redox transitions between oxygen intermediates in cytochrome-c oxidase. Proc Natl Acad Sci U S A 93: 12235-12239, 1996.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 12235-12239
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 244
    • 0035912857 scopus 로고    scopus 로고
    • Charge translocation coupled to electron injection into oxidized cytochrome c oxidase from Paracoccus denitrificans
    • Verkhovsky MI, Tuukkanen A, Backgren C, Puustinen A, and Wikström M. Charge translocation coupled to electron injection into oxidized cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 40: 7077-7083, 2001.
    • (2001) Biochemistry , vol.40 , pp. 7077-7083
    • Verkhovsky, M.I.1    Tuukkanen, A.2    Backgren, C.3    Puustinen, A.4    Wikström, M.5
  • 245
    • 0024515840 scopus 로고
    • Effect of pH on the spectrum of cytochrome c oxidase hydrogen peroxide complex
    • Vygodina T and Konstantinov A. Effect of pH on the spectrum of cytochrome c oxidase hydrogen peroxide complex. Biochim Biophys Acta 973: 390-398, 1989.
    • (1989) Biochim Biophys Acta , vol.973 , pp. 390-398
    • Vygodina, T.1    Konstantinov, A.2
  • 246
    • 0024346661 scopus 로고
    • 2-induced conversion of cytochrome c oxidase peroxy complex to oxoferryl state
    • 2-induced conversion of cytochrome c oxidase peroxy complex to oxoferryl state. Ann N Y Acad Sci 550: 124-138, 1988.
    • (1988) Ann N Y Acad Sci , vol.550 , pp. 124-138
    • Vygodina, T.V.1    Konstantinov, A.A.2
  • 247
    • 0039242661 scopus 로고
    • Energy-dependent reversal of the cytochrome oxidase reaction
    • Wikström M. Energy-dependent reversal of the cytochrome oxidase reaction. Proc Natl Acad Sci U S A 78: 4051-4054, 1981.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 4051-4054
    • Wikström, M.1
  • 248
    • 0021769852 scopus 로고
    • Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone
    • Wikström M. Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone. FEBS Lett 169: 300-304, 1984.
    • (1984) FEBS Lett , vol.169 , pp. 300-304
    • Wikström, M.1
  • 249
    • 0024571740 scopus 로고
    • Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping
    • Wikström M. Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping. Nature 338: 776-778, 1989.
    • (1989) Nature , vol.338 , pp. 776-778
    • Wikström, M.1
  • 250
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases
    • Wikström M, Jasaitis A, Backgren C, Puustinen A, and Verkhovsky MI. The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases. Biochim Biophys Acta 1459: 514-520, 2000.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 514-520
    • Wikström, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 252
    • 0026671804 scopus 로고
    • The dioxygen cycle: Spectral, kinetic, and thermodynamic characteristics of ferryl and peroxy intermediates observed by reversal of the cytochrome oxidase reaction
    • Wikström M and Morgan JE. The dioxygen cycle: spectral, kinetic, and thermodynamic characteristics of ferryl and peroxy intermediates observed by reversal of the cytochrome oxidase reaction. J Biol Chem 267: 10266-10273, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 10266-10273
    • Wikström, M.1    Morgan, J.E.2
  • 254
    • 0037726809 scopus 로고    scopus 로고
    • Water-gated mechanism of proton translocation by cytochrome c oxidase
    • Wikström M, Verkhovsky MI, and Hummer G. Water-gated mechanism of proton translocation by cytochrome c oxidase. Biochim Biophys Acta 1604: 61-65, 2003.
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 61-65
    • Wikström, M.1    Verkhovsky, M.I.2    Hummer, G.3
  • 255
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • Wikström MK. Proton pump coupled to cytochrome c oxidase in mitochondria. Nature 266: 271-273, 1977.
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.K.1
  • 256
    • 0017751901 scopus 로고
    • The mechanism of energy conservation and transduction by mitochondrial cytochrome c oxidase
    • Wikström MK and Saari HT. The mechanism of energy conservation and transduction by mitochondrial cytochrome c oxidase. Biochim Biophys Acta 462: 347-361, 1977.
    • (1977) Biochim Biophys Acta , vol.462 , pp. 347-361
    • Wikström, M.K.1    Saari, H.T.2
  • 257
    • 0017198072 scopus 로고
    • Some properties of the redox components of cytochrome c oxidase and their interactions
    • Wilson DF, Erecinska M, and Owen CS. Some properties of the redox components of cytochrome c oxidase and their interactions. Arch Biochem Biophys 175: 160-172, 1976.
    • (1976) Arch Biochem Biophys , vol.175 , pp. 160-172
    • Wilson, D.F.1    Erecinska, M.2    Owen, C.S.3
  • 258
    • 0020486275 scopus 로고
    • Coulometric and potentiometric evaluation of the redox components of cytochrome c oxidase in situ
    • Wilson DF and Nelson D. Coulometric and potentiometric evaluation of the redox components of cytochrome c oxidase in situ. Biochim Biophys Acta 680: 233-241, 1982.
    • (1982) Biochim Biophys Acta , vol.680 , pp. 233-241
    • Wilson, D.F.1    Nelson, D.2
  • 259
    • 0031054250 scopus 로고    scopus 로고
    • Isolation, analysis, and deletion of the gene coding for subunit IV of cytochrome c oxidase in Paracoccus denitrificans
    • Witt H and Ludwig B. Isolation, analysis, and deletion of the gene coding for subunit IV of cytochrome c oxidase in Paracoccus denitrificans. J Biol Chem 272: 5514-5517, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 5514-5517
    • Witt, H.1    Ludwig, B.2
  • 260
    • 0032570589 scopus 로고    scopus 로고
    • Tryptophan 121 of subunit II is the electron entry site to cytochrome c oxidase in Paracoccus denitrificans: Involvement of a hydrophobic patch in the docking reaction
    • Witt H, Malatesta F, Nicoletti F, Brunori M, and Ludwig B. Tryptophan 121 of subunit II is the electron entry site to cytochrome c oxidase in Paracoccus denitrificans: involvement of a hydrophobic patch in the docking reaction. J Biol Chem 273: 5132-5136, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 5132-5136
    • Witt, H.1    Malatesta, F.2    Nicoletti, F.3    Brunori, M.4    Ludwig, B.5
  • 262
    • 0021380356 scopus 로고
    • Formation and reduction of a "peroxy" intermediate of cytochrome c oxidase by hydrogen peroxide
    • Wrigglesworth JM. Formation and reduction of a "peroxy" intermediate of cytochrome c oxidase by hydrogen peroxide. Biochem J 217: 715-719, 1984.
    • (1984) Biochem J , vol.217 , pp. 715-719
    • Wrigglesworth, J.M.1
  • 263
    • 0032491195 scopus 로고    scopus 로고
    • Novel function of the regulatory subunit of protein kinase A: Regulation of cytochrome c oxidase activity and cytochrome c release
    • Yang WL, Iacono L, Tang WM, and Chin KV. Novel function of the regulatory subunit of protein kinase A: regulation of cytochrome c oxidase activity and cytochrome c release. Biochemistry 37: 14175-14180, 1998.
    • (1998) Biochemistry , vol.37 , pp. 14175-14180
    • Yang, W.L.1    Iacono, L.2    Tang, W.M.3    Chin, K.V.4
  • 264
    • 0036803084 scopus 로고    scopus 로고
    • The energy-transducing NADH: Quinone oxidoreductase, complex I
    • Yano T. The energy-transducing NADH: quinone oxidoreductase, complex I. Mol Aspects Med 23: 345-368, 2002.
    • (2002) Mol Aspects Med , vol.23 , pp. 345-368
    • Yano, T.1
  • 267
    • 0032552970 scopus 로고    scopus 로고
    • Single electron reduction of cytochrome c oxidase compound F: Resolution of partial steps by transient spectroscopy
    • Zaslavsky D, Sadoski RC, Wang K, Durham B, Gennis RB, and Millett F. Single electron reduction of cytochrome c oxidase compound F: resolution of partial steps by transient spectroscopy. Biochemistry 37: 14910-14916, 1998.
    • (1998) Biochemistry , vol.37 , pp. 14910-14916
    • Zaslavsky, D.1    Sadoski, R.C.2    Wang, K.3    Durham, B.4    Gennis, R.B.5    Millett, F.6
  • 268
    • 34250825264 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species-mediated signaling in endothelial cells
    • Zhang DX and Gutterman DD. Mitochondrial reactive oxygen species-mediated signaling in endothelial cells. Am J Physiol Heart Circ Physiol 292: H2023-H2031, 2007.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Zhang, D.X.1    Gutterman, D.D.2


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