메뉴 건너뛰기




Volumn 1757, Issue 9-10, 2006, Pages 1133-1143

Concerted involvement of cooperative proton-electron linkage and water production in the proton pump of cytochrome c oxidase

Author keywords

Cooperative H+ e linkage; Cytochrome c oxidase; Proton pump

Indexed keywords

CYTOCHROME C OXIDASE; HEME; IRON DERIVATIVE; PROTON PUMP; WATER;

EID: 33748954093     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.04.009     Document Type: Review
Times cited : (17)

References (55)
  • 1
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., and Changeux J.P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12 (1965) 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 2
    • 0016997305 scopus 로고
    • Haemoglobin: structure, function and synthesis
    • Perutz M.F. Haemoglobin: structure, function and synthesis. Br. Med. Bull. 32 (1976) 193-194
    • (1976) Br. Med. Bull. , vol.32 , pp. 193-194
    • Perutz, M.F.1
  • 3
    • 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 (1961) 144-148
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 5
    • 0015899089 scopus 로고
    • Proton translocation and energy transduction in mitochondria
    • Papa S., Guerrieri F., Lorusso M., and Simone S. Proton translocation and energy transduction in mitochondria. Biochemie 55 (1973) 703-716
    • (1973) Biochemie , vol.55 , pp. 703-716
    • Papa, S.1    Guerrieri, F.2    Lorusso, M.3    Simone, S.4
  • 6
    • 0017262329 scopus 로고
    • Proton translocation reactions in respiratory chains
    • Papa S. Proton translocation reactions in respiratory chains. Biochim. Biophys. Acta 456 (1976) 39-84
    • (1976) Biochim. Biophys. Acta , vol.456 , pp. 39-84
    • Papa, S.1
  • 8
    • 1942472486 scopus 로고    scopus 로고
    • Cytochrome c oxidase: 25 years of the elusive proton pump
    • Wikstrom M. Cytochrome c oxidase: 25 years of the elusive proton pump. Biochim. Biophys. Acta 1655 (2003) 241-247
    • (2003) Biochim. Biophys. Acta , vol.1655 , pp. 241-247
    • Wikstrom, M.1
  • 9
    • 3242763877 scopus 로고    scopus 로고
    • Redox-driven membrane-bound proton pumps
    • Brzezinski P. Redox-driven membrane-bound proton pumps. Trends Biochem. Sci. 29 (2004) 380-387
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 380-387
    • Brzezinski, P.1
  • 10
    • 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 (1976) 327-367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 11
    • 0033515466 scopus 로고    scopus 로고
    • Ubiquinol: cytochrome c oxidoreductase. Effects of inhibitors on reverse electron transfer from the iron-sulfur protein to cytochrome b
    • Matsumo-Yagi A., and Hatefi Y. Ubiquinol: cytochrome c oxidoreductase. Effects of inhibitors on reverse electron transfer from the iron-sulfur protein to cytochrome b. J. Biol. Chem. 274 (1999) 9283-9288
    • (1999) J. Biol. Chem. , vol.274 , pp. 9283-9288
    • Matsumo-Yagi, A.1    Hatefi, Y.2
  • 12
    • 33745605920 scopus 로고
    • Protonmotive ubiquinol-cytochrome c oxidoreductase of mitochondria. A possible example of co-operative anisotropy of protolytic redox catalysis
    • Lenaz G., Barnabei O., Rabbi A., and Battino M. (Eds), Taylor & Francis Ltd., London
    • Papa S., Lorusso M., Cocco T., Boffoli D., and Lombardo M. Protonmotive ubiquinol-cytochrome c oxidoreductase of mitochondria. A possible example of co-operative anisotropy of protolytic redox catalysis. In: Lenaz G., Barnabei O., Rabbi A., and Battino M. (Eds). Highlights in Ubiquinone Research (1990), Taylor & Francis Ltd., London 122-135
    • (1990) Highlights in Ubiquinone Research , pp. 122-135
    • Papa, S.1    Lorusso, M.2    Cocco, T.3    Boffoli, D.4    Lombardo, M.5
  • 13
    • 0038392255 scopus 로고    scopus 로고
    • Proton pumping by NADH: ubiquinone oxidoreductase. A redox driven conformational change mechanism?
    • Brandt U., Kersher S., Drose S., Zwicker K., and Zickermann V. Proton pumping by NADH: ubiquinone oxidoreductase. A redox driven conformational change mechanism?. FEBS Lett. 545 (2003) 9-17
    • (2003) FEBS Lett. , vol.545 , pp. 9-17
    • Brandt, U.1    Kersher, S.2    Drose, S.3    Zwicker, K.4    Zickermann, V.5
  • 14
    • 0033576277 scopus 로고    scopus 로고
    • Cytochrome c Oxidase: Catalytic Cycle and Mechanisms of Proton Pumping - a Discussion
    • Michel H. Cytochrome c Oxidase: Catalytic Cycle and Mechanisms of Proton Pumping - a Discussion. Biochemistry 38 (1999) 15129-15140
    • (1999) Biochemistry , vol.38 , pp. 15129-15140
    • Michel, H.1
  • 15
    • 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 (2003) 1-13
    • (2003) Biochim. Biophys. Acta , vol.1605 , pp. 1-13
    • Brzezinski, P.1    Larsson, G.2
  • 16
    • 1942472174 scopus 로고    scopus 로고
    • A cooperative model for proton pumping in cytochrome c oxidase
    • Papa S., Capitanio N., and Capitanio G. A cooperative model for proton pumping in cytochrome c oxidase. Biochim. Biophys. Acta. 1655 (2004) 353-364
    • (2004) Biochim. Biophys. Acta. , vol.1655 , pp. 353-364
    • Papa, S.1    Capitanio, N.2    Capitanio, G.3
  • 18
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper Terminal Oxidases
    • Ferguson-Miller S., and Babcock G.T. Heme/copper Terminal Oxidases. Chem. Rev. 96 (1996) 2889-2908
    • (1996) Chem. Rev. , vol.96 , pp. 2889-2908
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 19
    • 0019363133 scopus 로고
    • Proton-translocating cytochrome complexes
    • Wikstrom M., Krab K., and Saraste M. Proton-translocating cytochrome complexes. Ann. Rev. Biochem. 50 (1981) 623-655
    • (1981) Ann. Rev. Biochem. , vol.50 , pp. 623-655
    • Wikstrom, M.1    Krab, K.2    Saraste, M.3
  • 20
    • 0029783621 scopus 로고    scopus 로고
    • Factors affecting the H+/e- stoichiometry in mitochondrial cytochrome c oxidase: influence of the rate of electron flow and transmembrane delta pH
    • Capitanio N., Capitanio G., Demarinis D.A., De Nitto E., Massari S., and Papa S. Factors affecting the H+/e- stoichiometry in mitochondrial cytochrome c oxidase: influence of the rate of electron flow and transmembrane delta pH. Biochemistry 35 (1996) 10800-10806
    • (1996) Biochemistry , vol.35 , pp. 10800-10806
    • Capitanio, N.1    Capitanio, G.2    Demarinis, D.A.3    De Nitto, E.4    Massari, S.5    Papa, S.6
  • 21
    • 0039840998 scopus 로고    scopus 로고
    • Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides
    • Junemann S., Meunier B., Gennis R.B., and Rich P.R. Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 36 (1997) 14456-14464
    • (1997) Biochemistry , vol.36 , pp. 14456-14464
    • Junemann, S.1    Meunier, B.2    Gennis, R.B.3    Rich, P.R.4
  • 23
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxen K., Gilderson G., Adelroth P., and Brzezinski P. A mechanistic principle for proton pumping by cytochrome c oxidase. Nature 437 (2005) 286-289
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxen, K.1    Gilderson, G.2    Adelroth, P.3    Brzezinski, P.4
  • 25
    • 17144386974 scopus 로고    scopus 로고
    • B in the proton pump of cytochrome c oxidase
    • B in the proton pump of cytochrome c oxidase. Biochemistry (Moscow) 70 (2005) 178-186
    • (2005) Biochemistry (Moscow) , vol.70 , pp. 178-186
    • Papa, S.1
  • 26
    • 0017883558 scopus 로고
    • Involvement of intramitochondrial protons in redox reactions of cytochrome alpha
    • Artzatbanov V.Y., Konstantinov A.A., and Skulachev V.P. Involvement of intramitochondrial protons in redox reactions of cytochrome alpha. FEBS Lett. 87 (1978) 180-185
    • (1978) FEBS Lett. , vol.87 , pp. 180-185
    • Artzatbanov, V.Y.1    Konstantinov, A.A.2    Skulachev, V.P.3
  • 28
    • 0021099512 scopus 로고
    • Redox-linked hydrogen bond strength changes in cytochrome a: implications for a cytochrome oxidase proton pump
    • Babcock G.T., and Callahan P.M. Redox-linked hydrogen bond strength changes in cytochrome a: implications for a cytochrome oxidase proton pump. Biochemistry 22 (1983) 2314-2319
    • (1983) Biochemistry , vol.22 , pp. 2314-2319
    • Babcock, G.T.1    Callahan, P.M.2
  • 29
    • 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 (1998) 1-8
    • (1998) FEBS Lett. , vol.439 , pp. 1-8
    • Papa, S.1    Capitanio, N.2    Villani, G.3
  • 32
    • 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., Mantele 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 (1999) 37974-37981
    • (1999) J. Biol. Chem. , vol.274 , pp. 37974-37981
    • Kannt, A.1    Pfitzner, U.2    Ruitenberg, M.3    Hellwig, P.4    Ludwig, B.5    Mantele, W.6    Fendler, K.7    Michel, H.8
  • 33
    • 0033856862 scopus 로고    scopus 로고
    • Redox-linked conformational changes in bovine heart cytochrome c oxidase: picosecond time-resolved fluorescence studies of cyanide complex
    • Das T.K., and Mazumdar S. Redox-linked conformational changes in bovine heart cytochrome c oxidase: picosecond time-resolved fluorescence studies of cyanide complex. Biopolymers 57 (2000) 316-322
    • (2000) Biopolymers , vol.57 , pp. 316-322
    • Das, T.K.1    Mazumdar, S.2
  • 34
    • 33745633994 scopus 로고    scopus 로고
    • Non resonance Raman spectroscopic analysis of heme-copper oxidases: characterization of a heme a redox state marker
    • (EBEC Short reports Supplement)
    • Capitanio N., Piccoli C., Capitanio G., Perna G., Boffoli D., Capozzi V., and Papa S. Non resonance Raman spectroscopic analysis of heme-copper oxidases: characterization of a heme a redox state marker. Biochim. Biophys. Acta Bioenerg. 13 (2004) 149 (EBEC Short reports Supplement)
    • (2004) Biochim. Biophys. Acta Bioenerg. , vol.13 , pp. 149
    • Capitanio, N.1    Piccoli, C.2    Capitanio, G.3    Perna, G.4    Boffoli, D.5    Capozzi, V.6    Papa, S.7
  • 36
    • 0023000170 scopus 로고
    • Accessibility of the cytochrome a heme in cytochrome c oxidase to exchangeable protons
    • Argade P.V., Ching Y.C., Sassaroli M., and Rousseau D.L. Accessibility of the cytochrome a heme in cytochrome c oxidase to exchangeable protons. J. Biol. Chem. 261 (1986) 5969-5973
    • (1986) J. Biol. Chem. , vol.261 , pp. 5969-5973
    • Argade, P.V.1    Ching, Y.C.2    Sassaroli, M.3    Rousseau, D.L.4
  • 38
    • 0016173383 scopus 로고
    • Redox potentiometry in mitochondrial and photosynthetic bioenergetics
    • Dutton P.L., and Wilson D.F. Redox potentiometry in mitochondrial and photosynthetic bioenergetics. Biochim. Biophys. Acta 346 (1974) 165-212
    • (1974) Biochim. Biophys. Acta , vol.346 , pp. 165-212
    • Dutton, P.L.1    Wilson, D.F.2
  • 40
    • 0037195262 scopus 로고    scopus 로고
    • Redox-linked protonation of cytochrome c oxidase: the effect of chloride bound to CuB
    • Forte E., Barone M.C., Brunori M., Sarti P., and Giuffre A. Redox-linked protonation of cytochrome c oxidase: the effect of chloride bound to CuB. Biochemistry 41 (2002) 13046-13052
    • (2002) Biochemistry , vol.41 , pp. 13046-13052
    • Forte, E.1    Barone, M.C.2    Brunori, M.3    Sarti, P.4    Giuffre, A.5
  • 42
    • 0022484362 scopus 로고
    • Spectroelectrochemical study of the cytochrome a site in carbon monoxide inhibited cytochrome c oxidase
    • Ellis Jr. W.R., Wang H., Blair D.F., Gray H.B., and Chan S.I. Spectroelectrochemical study of the cytochrome a site in carbon monoxide inhibited cytochrome c oxidase. Biochemistry 25 (1986) 161-167
    • (1986) Biochemistry , vol.25 , pp. 161-167
    • Ellis Jr., W.R.1    Wang, H.2    Blair, D.F.3    Gray, H.B.4    Chan, S.I.5
  • 43
    • 32344440421 scopus 로고
    • On the mechanism of proton pumps in respiratory chains
    • Papa S., and Tager J.M. (Eds), Birkhauser Verlag Basel, Switzerland
    • Papa S., Lorusso M., and Capitanio N. On the mechanism of proton pumps in respiratory chains. In: Papa S., and Tager J.M. (Eds). Biochemistry of Cell Membranes (1995), Birkhauser Verlag Basel, Switzerland 151-166
    • (1995) Biochemistry of Cell Membranes , pp. 151-166
    • Papa, S.1    Lorusso, M.2    Capitanio, N.3
  • 44
    • 0022550138 scopus 로고
    • Intrinsic uncoupling of mitochondrial proton pumps. 2. Modeling studies
    • Pietrobon D., Zoratti M., Azzone G.F., and Caplan S.R. Intrinsic uncoupling of mitochondrial proton pumps. 2. Modeling studies. Biochemistry 25 (1986) 767-775
    • (1986) Biochemistry , vol.25 , pp. 767-775
    • Pietrobon, D.1    Zoratti, M.2    Azzone, G.F.3    Caplan, S.R.4
  • 45
    • 0242600563 scopus 로고    scopus 로고
    • Proton transfer reactions associated with the reaction of the fully reduced, purified cytochrome c oxidase with molecular oxygen and ferricyanide
    • Capitanio N., Capitanio G., De Nitto E., Boffoli D., and Papa S. Proton transfer reactions associated with the reaction of the fully reduced, purified cytochrome c oxidase with molecular oxygen and ferricyanide. Biochemistry 42 (2003) 4607-4612
    • (2003) Biochemistry , vol.42 , pp. 4607-4612
    • Capitanio, N.1    Capitanio, G.2    De Nitto, E.3    Boffoli, D.4    Papa, S.5
  • 48
    • 0028813330 scopus 로고
    • Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases
    • Rich P.R. Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases. Aust. J. Plant. Physiol. 22 (1995) 479-486
    • (1995) Aust. J. Plant. Physiol. , vol.22 , pp. 479-486
    • Rich, P.R.1
  • 50
    • 0024571740 scopus 로고
    • Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping
    • Wikstrom M. Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping. Nature 338 (1989) 776-778
    • (1989) Nature , vol.338 , pp. 776-778
    • Wikstrom, M.1
  • 51
    • 0034727649 scopus 로고    scopus 로고
    • Formation of the "peroxy" intermediate in cytochrome c oxidase is associated with internal proton/hydrogen transfer
    • Karpefors M., Adelroth 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 (2000) 14664-14669
    • (2000) Biochemistry , vol.39 , pp. 14664-14669
    • Karpefors, M.1    Adelroth, P.2    Namslauer, A.3    Zhen, Y.4    Brzezinski, P.5
  • 52
    • 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 M.I., Morgan J.E., Verkhovskaya M.L., and Wikstrom M. Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen. Biochemistry 38 (1999) 2697-2706
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Verkhovskaya, M.L.4    Wikstrom, M.5
  • 54
    • 0037726805 scopus 로고    scopus 로고
    • Intrinsic and extrinsic uncoupling of oxidative phosphorylation
    • Kadenbach B. Intrinsic and extrinsic uncoupling of oxidative phosphorylation. Biochim. Biophys. Acta 1604 (2003) 77-94
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 77-94
    • Kadenbach, B.1
  • 55
    • 33745622830 scopus 로고    scopus 로고
    • Cooperativity and flexibility of the protonmotive activity of mitochondrial respiratory chain
    • Papa S., Lorusso M., and Di Paola M. Cooperativity and flexibility of the protonmotive activity of mitochondrial respiratory chain. Biochim. Biophys. Acta 1757 (2006) 428-438
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 428-438
    • Papa, S.1    Lorusso, M.2    Di Paola, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.