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Volumn 1655, Issue 1-3, 2004, Pages 353-364

A cooperative model for proton pumping in cytochrome c oxidase

Author keywords

Cooperativity; Cytochrome c oxidase; Mitochondria; Proton pumping

Indexed keywords

CYTOCHROME C OXIDASE; PROTON PUMP;

EID: 1942472174     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.06.002     Document Type: Review
Times cited : (28)

References (60)
  • 2
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism
    • Mitchell P. Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism. Nature. 191:1961;144.
    • (1961) Nature , vol.191 , pp. 144
    • Mitchell, P.1
  • 3
    • 0018784261 scopus 로고
    • Keilin's respiratory chain concept and its chemiosmotic consequences
    • Mitchell P. Keilin's respiratory chain concept and its chemiosmotic consequences. Science. 206:1979;1148-1159.
    • (1979) Science , vol.206 , pp. 1148-1159
    • Mitchell, P.1
  • 5
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 6
    • 0034678612 scopus 로고    scopus 로고
    • Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from Thermus thermophilus
    • Soulimane T., Buse G., Bourenkov G.P., Bartunik H.D., Huber R., Than M.E. Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from Thermus thermophilus. EMBO J. 19:2000;1766-1776.
    • (2000) EMBO J. , vol.19 , pp. 1766-1776
    • Soulimane, T.1    Buse, G.2    Bourenkov, G.P.3    Bartunik, H.D.4    Huber, R.5    Than, M.E.6
  • 7
    • 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., Iwata S. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321:2002;329-339.
    • (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
  • 12
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J., Wyman J., 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
  • 14
    • 0035814137 scopus 로고    scopus 로고
    • Cooperativity between electrons and protons in monomeric cytochrome c(3): The importance of mechano-chemical coupling for energy transduction
    • Louro R.O., Catarino T., LeGall J., Turner D.L., Xavier A.V. Cooperativity between electrons and protons in monomeric cytochrome c(3): the importance of mechano-chemical coupling for energy transduction. ChemBioChem. 2:2001;22-28.
    • (2001) ChemBioChem , vol.2 , pp. 22-28
    • Louro, R.O.1    Catarino, T.2    Legall, J.3    Turner, D.L.4    Xavier, A.V.5
  • 16
    • 0016173383 scopus 로고
    • Redox potentiometry in mitochondrial and photosynthetic bioenergetics
    • Dutton P.L., 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
  • 17
    • 0015899089 scopus 로고
    • Proton translocation and energy transduction in mitochondria
    • Papa S., Guerrieri F., Lorusso M., Simone S. Proton translocation and energy transduction in mitochondria. Biochimie. 55:1973;703-716.
    • (1973) Biochimie , vol.55 , pp. 703-716
    • Papa, S.1    Guerrieri, F.2    Lorusso, M.3    Simone, S.4
  • 18
    • 0017262329 scopus 로고
    • Proton translocation reactions in the respiratory chain
    • Papa S. Proton translocation reactions in the respiratory chain. Biochim. Biophys. Acta. 456:1976;39-84.
    • (1976) Biochim. Biophys. Acta , vol.456 , pp. 39-84
    • Papa, S.1
  • 20
    • 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
  • 21
    • 0034640452 scopus 로고    scopus 로고
    • Mechanism of proton translocation by cytochrome c oxidase: A new four-stroke histidine cycle
    • Wikstrom M. Mechanism of proton translocation by cytochrome c oxidase: a new four-stroke histidine cycle. Biochim. Biophys. Acta. 1458:2000;188-198.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 188-198
    • Wikstrom, M.1
  • 22
    • 0021099512 scopus 로고
    • Redox-linked hydrogen bond strength changes in cytochrome a: Implications for a cytochrome oxidase proton pump
    • Babcock G.T., 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
  • 25
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • Pereira M.M., Santana M., Teixeira M. A novel scenario for the evolution of haem-copper oxygen reductases. Biochim. Biophys. Acta. 1505:2001;185-208.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 26
  • 29
    • 0025060363 scopus 로고
    • Cytochrome c oxidase: Understanding nature's design of a proton pump
    • Chan S.I., Li P.M. Cytochrome c oxidase: understanding nature's design of a proton pump. Biochemistry. 29:1990;1-12.
    • (1990) Biochemistry , vol.29 , pp. 1-12
    • Chan, S.I.1    Li, P.M.2
  • 30
    • 0017883558 scopus 로고
    • Involvement of intramitochondrial protons in redox reactions of cytochrome alpha
    • Artzatbanov V.Y., Konstantinov A.A., 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
  • 33
    • 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., 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
  • 34
    • 0034663697 scopus 로고    scopus 로고
    • Protonation reactions in relation to the coupling mechanism of bovine cytochrome c oxidase
    • Rich P.R., Breton J., Junemann S., Heathcote P. Protonation reactions in relation to the coupling mechanism of bovine cytochrome c oxidase. Biochim. Biophys. Acta. 1459:2000;475-480.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 475-480
    • Rich, P.R.1    Breton, J.2    Junemann, S.3    Heathcote, P.4
  • 35
    • 0037014585 scopus 로고    scopus 로고
    • Plasticity of proton pathways in haem-copper oxygen reductases
    • Pereira M.M., Gomes C.M., Teixeira M. Plasticity of proton pathways in haem-copper oxygen reductases. FEBS Lett. 522:2002;14-18.
    • (2002) FEBS Lett. , vol.522 , pp. 14-18
    • Pereira, M.M.1    Gomes, C.M.2    Teixeira, M.3
  • 36
    • 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 H.M., Das T.K., Rousseau D.L., Mills D., Ferguson-Miller S., Gennis R.B. 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. 39:2000;2989-2996.
    • (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
  • 37
    • 0031973948 scopus 로고    scopus 로고
    • Oxygen and proton pathways in cytochrome c oxidase
    • Hofacker I., Schulten K. Oxygen and proton pathways in cytochrome c oxidase. Proteins. 30:1998;100-107.
    • (1998) Proteins , vol.30 , pp. 100-107
    • Hofacker, I.1    Schulten, K.2
  • 39
    • 0022484362 scopus 로고
    • Spectroelectrochemical study of the cytochrome a site in carbon monoxide inhibited cytochrome c oxidase
    • Ellis W.R. Jr., Wang H., Blair D.F., Gray H.B., 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, W.R.Jr.1    Wang, H.2    Blair, D.F.3    Gray, H.B.4    Chan, S.I.5
  • 41
    • 0025017007 scopus 로고
    • Rapid proton release during flash-induced oxidation of cytochrome c oxidase
    • Nilsson T., Hallén S., Oliveberg M. Rapid proton release during flash-induced oxidation of cytochrome c oxidase. FEBS Lett. 260:1990;45-47.
    • (1990) FEBS Lett. , vol.260 , pp. 45-47
    • Nilsson, T.1    Hallén, S.2    Oliveberg, M.3
  • 42
    • 0025981255 scopus 로고
    • Uptake and release of protons during the reaction between cytochrome c oxidase and molecular oxygen: A flow-flash investigation
    • Oliveberg M., Hallén S., Nilsson T. Uptake and release of protons during the reaction between cytochrome c oxidase and molecular oxygen: a flow-flash investigation. Biochemistry. 30:1991;436-440.
    • (1991) Biochemistry , vol.30 , pp. 436-440
    • Oliveberg, M.1    Hallén, S.2    Nilsson, T.3
  • 44
    • 0242600563 scopus 로고    scopus 로고
    • Proton transfer reactions associated with the fully reduced, purified cytochrome c oxidase with molecular oxygen and ferricyanide
    • Capitanio N., Capitanio G., De Nitto E., Boffoli D., Papa S. Proton transfer reactions associated with 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
  • 45
    • 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., Michel H. Reduction of cytochrome c oxidase by a second electron leads to proton translocation. Nature. 417:2002;99-102.
    • (2002) Nature , vol.417 , pp. 99-102
    • Ruitenberg, M.1    Kannt, A.2    Bamberg, E.3    Fendler, K.4    Michel, H.5
  • 46
    • 0033741298 scopus 로고    scopus 로고
    • X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase
    • Yoshikawa S., Shinzawa-Itoh K., Tsukihara T. X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase. J. Inorg. Biochem. 82:2000;1-7.
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 1-7
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Tsukihara, T.3
  • 47
    • 0000540212 scopus 로고
    • Proton exchange in amides: Surprise from simple systems
    • Perrin C.L. Proton exchange in amides: surprise from simple systems. Acc. Chem. Res. 22:1989;268-275.
    • (1989) Acc. Chem. Res. , vol.22 , pp. 268-275
    • Perrin, C.L.1
  • 48
    • 0037156879 scopus 로고    scopus 로고
    • Electron transfer at the low-spin heme b of cytochrome bo(3) induces an environmental change of the catalytic enhancer glutamic acid-286
    • Prutsch A., Vogtt K., Ludovici C., Lubben M. Electron transfer at the low-spin heme b of cytochrome bo(3) induces an environmental change of the catalytic enhancer glutamic acid-286. Biochim. Biophys. Acta. 1554:2002;22-28.
    • (2002) Biochim. Biophys. Acta , vol.1554 , pp. 22-28
    • Prutsch, A.1    Vogtt, K.2    Ludovici, C.3    Lubben, M.4
  • 49
    • 0024522067 scopus 로고
    • Cytochrome c oxidase: Evidence for interaction of water molecules with cytochrome a
    • Sassaroli M., Ching Y.C., Dasgupta S., Rousseau D.L. Cytochrome c oxidase: evidence for interaction of water molecules with cytochrome a. Biochemistry. 28:1989;3128-3132.
    • (1989) Biochemistry , vol.28 , pp. 3128-3132
    • Sassaroli, M.1    Ching, Y.C.2    Dasgupta, S.3    Rousseau, D.L.4
  • 50
    • 0037132542 scopus 로고    scopus 로고
    • A mechano-chemical model for energy transduction in cytochrome c oxidase: The work of a Maxwell's god
    • Xavier A.V. A mechano-chemical model for energy transduction in cytochrome c oxidase: the work of a Maxwell's god. FEBS Lett. 532:2002;261-266.
    • (2002) FEBS Lett. , vol.532 , pp. 261-266
    • Xavier, A.V.1
  • 51
    • 0000816133 scopus 로고
    • The oxidation-reduction potential of the copper signal in pigeon heart mitochondria
    • Erecinska M., Chance B., Wilson D.F. The oxidation-reduction potential of the copper signal in pigeon heart mitochondria. FEBS Lett. 16:1971;284-286.
    • (1971) FEBS Lett. , vol.16 , pp. 284-286
    • Erecinska, M.1    Chance, B.2    Wilson, D.F.3
  • 53
    • 0028855258 scopus 로고
    • Rapid kinetics of membrane potential generation by cytochrome c oxidase with the photoactive Ru(II)-tris-bipyridyl derivative of cytochrome c as electron donor
    • Zaslavsky D.L., Smirnova I.A., Siletsky S.A., Kaulen A.D., Millett F., Konstantinov A.A. Rapid kinetics of membrane potential generation by cytochrome c oxidase with the photoactive Ru(II)-tris-bipyridyl derivative of cytochrome c as electron donor. FEBS Lett. 359:1995;27-30.
    • (1995) FEBS Lett. , vol.359 , pp. 27-30
    • Zaslavsky, D.L.1    Smirnova, I.A.2    Siletsky, S.A.3    Kaulen, A.D.4    Millett, F.5    Konstantinov, A.A.6
  • 54
    • 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., 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. 97:2000;4632-4636.
    • (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
  • 55
    • 1942537368 scopus 로고
    • Molecular code for cooperativity in hemoglobin
    • Ackers G.K., Doyle M.L., Myers D., Daugherty M.A. Molecular code for cooperativity in hemoglobin. Science. 256:1992;1684-1687.
    • (1992) Science , vol.256 , pp. 1684-1687
    • Ackers, G.K.1    Doyle, M.L.2    Myers, D.3    Daugherty, M.A.4
  • 56
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • Boyer P.D. The ATP synthase-a splendid molecular machine. Ann. Rev. Biochem. 66:1997;717-749.
    • (1997) Ann. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 58
    • 78651031094 scopus 로고
    • The mitochondrial cytochrome chain
    • Chance B., Williams G.R. The mitochondrial cytochrome chain. Adv. Enzymol. 17:1956;65-134.
    • (1956) Adv. Enzymol. , vol.17 , pp. 65-134
    • Chance, B.1    Williams, G.R.2
  • 59
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in complex I
    • Ohnishi T. Iron-sulfur clusters/semiquinones in complex I. Biochim. Biophys. Acta. 1364:1998;186-206.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 60
    • 0030730497 scopus 로고    scopus 로고
    • 1 complex is affected by the protonation state of a redox-Bohr group of the 'Rieske' iron-sulfur protein
    • 1 complex is affected by the protonation state of a redox-Bohr group of the 'Rieske' iron-sulfur protein. Biochim. Biophys. Acta. 1321:1997;238-242.
    • (1997) Biochim. Biophys. Acta , vol.1321 , pp. 238-242
    • Brandt, U.1    Djafarzadeh-Andabili, R.2


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