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Volumn 1757, Issue 8, 2006, Pages 1052-1063

Transmembrane proton translocation by cytochrome c oxidase

Author keywords

Cytochrome aa3; Electrochemical proton gradient; Electron transfer; Proton transfer; Quinol oxidase

Indexed keywords

COPPER; CYTOCHROME C OXIDASE; HEME; MEMBRANE PROTEIN; OXIDOREDUCTASE;

EID: 33749137961     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.05.020     Document Type: Review
Times cited : (116)

References (112)
  • 1
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochromecoxidase in mitochondria
    • Wikström M.K.F. Proton pump coupled to cytochromecoxidase in mitochondria. Nature 266 (1977) 271-273
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.K.F.1
  • 2
    • 0027160144 scopus 로고
    • Proton pumping by cytochrome oxidase as studied by time-resolved stopped-flow spectrophotometry
    • Antonini G., Malatesta F., Sarti P., and Brunori M. Proton pumping by cytochrome oxidase as studied by time-resolved stopped-flow spectrophotometry. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 5949-5953
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 5949-5953
    • Antonini, G.1    Malatesta, F.2    Sarti, P.3    Brunori, M.4
  • 5
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochromecoxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., and Michel H. Structure at 2.8 Å resolution of cytochromecoxidase 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
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochromecoxidases from Rhodobacter sphaeroides
    • Svensson-Ek M., Abramson J., Larsson G., Törnroth S., Brzezinski P., and Iwata S. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochromecoxidases 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    Törnroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 7
    • 0025801345 scopus 로고
    • The gene encoding cytochromecoxidase 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 cytochromecoxidase subunit II from Rhodobacter sphaeroides; comparison of the deduced amino acid sequence with sequences of corresponding peptides from other species. Gene 101 (1991) 133-137
    • (1991) Gene , vol.101 , pp. 133-137
    • Cao, J.1    Shapleigh, J.2    Gennis, R.3    Revzin, A.4    Ferguson-Miller, S.5
  • 8
    • 0026615058 scopus 로고
    • Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochromecoxidase. The coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast
    • Cao J., Hosler J., Shapleigh J., Revzin A., and Ferguson-Miller S. Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochromecoxidase. The coxII/coxIII operon codes for structural and assembly proteins homologous to those in yeast. J. Biol. Chem. 267 (1992) 24273-24278
    • (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
  • 9
    • 0026583053 scopus 로고
    • Cloning, sequencing and deletion from the chromosome of the gene encoding subunit I of the aa3-type cytochromecoxidase of Rhodobacter sphaeroides
    • Shapleigh J.P., and Gennis R.B. Cloning, sequencing and deletion from the chromosome of the gene encoding subunit I of the aa3-type cytochromecoxidase of Rhodobacter sphaeroides. Mol. Microbiol. 6 (1992) 635-642
    • (1992) Mol. Microbiol. , vol.6 , pp. 635-642
    • Shapleigh, J.P.1    Gennis, R.B.2
  • 10
    • 0026615057 scopus 로고
    • Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochromecoxidase. Purification, kinetics, proton pumping, and spectral analysis
    • Hosler J.P., Fetter J., Tecklenburg M.M., Espe M., Lerma C., and Ferguson-Miller S. Cytochrome aa3 of Rhodobacter sphaeroides as a model for mitochondrial cytochromecoxidase. Purification, kinetics, proton pumping, and spectral analysis. J. Biol. Chem. 267 (1992) 24264-24272
    • (1992) J. Biol. Chem. , vol.267 , pp. 24264-24272
    • Hosler, J.P.1    Fetter, J.2    Tecklenburg, M.M.3    Espe, M.4    Lerma, C.5    Ferguson-Miller, S.6
  • 11
  • 14
    • 0031776726 scopus 로고    scopus 로고
    • From NO to OO: nitric oxide and dioxygen in bacterial respiration
    • Hendriks J., Gohlke U., and Saraste M. From NO to OO: nitric oxide and dioxygen in bacterial respiration. J. Bioenerg. Biomembranes 30 (1998) 15-24
    • (1998) J. Bioenerg. Biomembranes , vol.30 , pp. 15-24
    • Hendriks, J.1    Gohlke, U.2    Saraste, M.3
  • 15
    • 0025879301 scopus 로고
    • Subunit III of cytochromecoxidase is not involved in proton translocation: a site-directed mutagenesis study
    • Haltia T., Saraste M., and Wikström M. Subunit III of cytochromecoxidase is not involved in proton translocation: a site-directed mutagenesis study. EMBO J. 10 (1991) 2015-2021
    • (1991) EMBO J. , vol.10 , pp. 2015-2021
    • Haltia, T.1    Saraste, M.2    Wikström, M.3
  • 16
    • 0025784931 scopus 로고
    • Comparison of energy-transducing capabilities of the 2-subunit and 3-subunit cytochromes Aa3 from paracoccus-denitrificans and the 13-subunit beef-heart enzyme
    • Hendler R.W., Pardhasaradhi K., Reynafarje B., and Ludwig B. Comparison of energy-transducing capabilities of the 2-subunit and 3-subunit cytochromes Aa3 from paracoccus-denitrificans and the 13-subunit beef-heart enzyme. Biophys. J. 60 (1991) 415-423
    • (1991) Biophys. J. , vol.60 , pp. 415-423
    • Hendler, R.W.1    Pardhasaradhi, K.2    Reynafarje, B.3    Ludwig, B.4
  • 17
    • 0034711013 scopus 로고    scopus 로고
    • Identification of the structural subunits required for formation of the metal centers in subunit I of cytochromecoxidase of Rhodobacter sphaeroides
    • Bratton M.R., Hiser L., Antholine W.E., Hoganson C., and Hosler J.P. Identification of the structural subunits required for formation of the metal centers in subunit I of cytochromecoxidase of Rhodobacter sphaeroides. Biochemistry 39 (2000) 12989-12995
    • (2000) Biochemistry , vol.39 , pp. 12989-12995
    • Bratton, M.R.1    Hiser, L.2    Antholine, W.E.3    Hoganson, C.4    Hosler, J.P.5
  • 18
    • 0023049138 scopus 로고
    • Transient kinetics of subunit-III-depleted cytochromecoxidase
    • Malatesta F., Antonini G., Sarti P., and Brunori M. Transient kinetics of subunit-III-depleted cytochromecoxidase. Biochem. J. 234 (1986) 569-572
    • (1986) Biochem. J. , vol.234 , pp. 569-572
    • Malatesta, F.1    Antonini, G.2    Sarti, P.3    Brunori, M.4
  • 19
    • 0022037634 scopus 로고
    • Cytochromecoxidase depleted of subunit III: proton-pumping, respiratory control, and pH dependence of the midpoint potential of cytochrome a
    • Thompson D.A., Gregory L., and Ferguson-Miller S. Cytochromecoxidase depleted of subunit III: proton-pumping, respiratory control, and pH dependence of the midpoint potential of cytochrome a. J. Inorg. Biochem. 23 (1985) 357-364
    • (1985) J. Inorg. Biochem. , vol.23 , pp. 357-364
    • Thompson, D.A.1    Gregory, L.2    Ferguson-Miller, S.3
  • 20
    • 0033534165 scopus 로고    scopus 로고
    • Suicide inactivation of cytochromecoxidase: catalytic turnover in the absence of subunit III alters the active site
    • Bratton M.R., Pressler M.A., and Hosler J.P. Suicide inactivation of cytochromecoxidase: catalytic turnover in the absence of subunit III alters the active site. Biochemistry 38 (1999) 16236-16245
    • (1999) Biochemistry , vol.38 , pp. 16236-16245
    • Bratton, M.R.1    Pressler, M.A.2    Hosler, J.P.3
  • 22
    • 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 R.B., 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 (2004) 11617-11621
    • (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
  • 24
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochromecoxidase 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 cytochromecoxidase complexed with an antibody FV fragment. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 10547-10553
    • (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
  • 28
    • 0026457361 scopus 로고
    • A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome-c-oxidase
    • Antholine W.E., Kastrau D.H.W., Steffens G.C.M., Buse G., Zumft W.G., and Kroneck P.M.H. A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome-c-oxidase. Eur. J. Biochem. 209 (1992) 875-881
    • (1992) Eur. J. Biochem. , vol.209 , pp. 875-881
    • Antholine, W.E.1    Kastrau, D.H.W.2    Steffens, G.C.M.3    Buse, G.4    Zumft, W.G.5    Kroneck, P.M.H.6
  • 29
    • 0032318376 scopus 로고    scopus 로고
    • Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine
    • Gennis R.B. Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine. Biochim. Biophys. Acta 1365 (1998) 241-248
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 241-248
    • Gennis, R.B.1
  • 30
    • 2442616154 scopus 로고    scopus 로고
    • Proton pumping mechanism and catalytic cycle of cytochromecoxidase: Coulomb pump model with kinetic gating
    • Popovic D.M., and Stuchebrukhov A.A. Proton pumping mechanism and catalytic cycle of cytochromecoxidase: Coulomb pump model with kinetic gating. FEBS Lett. 566 (2004) 126-130
    • (2004) FEBS Lett. , vol.566 , pp. 126-130
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 31
    • 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 (1999) 35-37
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 35-37
    • Puustinen, A.1    Wikström, M.2
  • 32
    • 0033576277 scopus 로고    scopus 로고
    • Cytochromecoxidase: catalytic cycle and mechanisms of proton pumping-A discussion
    • Michel H. Cytochromecoxidase: catalytic cycle and mechanisms of proton pumping-A discussion. Biochemistry 38 (1999) 15129-15140
    • (1999) Biochemistry , vol.38 , pp. 15129-15140
    • Michel, H.1
  • 33
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochromecoxidase
    • Kannt A., Roy C., Lancaster D., and Michel H. The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochromecoxidase. Biophys. J. 74 (1998) 708-721
    • (1998) Biophys. J. , vol.74 , pp. 708-721
    • Kannt, A.1    Roy, C.2    Lancaster, D.3    Michel, H.4
  • 34
    • 1242314254 scopus 로고    scopus 로고
    • Electrostatic study of the proton pumping mechanism in bovine heart cytochromecoxidase
    • Popovic D.M., and Stuchebrukhov A.A. Electrostatic study of the proton pumping mechanism in bovine heart cytochromecoxidase. J. Am. Chem. Soc. 126 (2004) 1858-1871
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1858-1871
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 35
    • 0032546616 scopus 로고    scopus 로고
    • Redox dependent changes at the heme propionates in cytochromecoxidase from paracoccus denitrificans: direct evidence from FTIR difference spectroscopy in combination with heme propionate 13c labeling
    • Behr J., Hellwig P., M.W., and Michel H. Redox dependent changes at the heme propionates in cytochromecoxidase from paracoccus denitrificans: direct evidence from FTIR difference spectroscopy in combination with heme propionate 13c labeling. Biochemistry 37 (1998) 7400-7406
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7400-7406
    • Behr, J.1    Hellwig, P.2    Mantele, W.3    Michel, H.4
  • 36
    • 0037726809 scopus 로고    scopus 로고
    • Water-gated mechanism of proton translocation by cytochrome c oxidase
    • Wikström M., Verkhovsky M.I., and Hummer G. Water-gated mechanism of proton translocation by cytochrome c oxidase. Biochim. Biophys. Acta 1604 (2003) 61-65
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 61-65
    • Wikström, M.1    Verkhovsky, M.I.2    Hummer, G.3
  • 37
    • 16344363592 scopus 로고    scopus 로고
    • Simulating redox coupled proton transfer in cytochromecoxidase: looking for the proton bottleneck
    • Olsson M.H.M., Sharma P.K., and Warshel A. Simulating redox coupled proton transfer in cytochromecoxidase: looking for the proton bottleneck. FEBS Lett. 579 (2005) 2026-2034
    • (2005) FEBS Lett. , vol.579 , pp. 2026-2034
    • Olsson, M.H.M.1    Sharma, P.K.2    Warshel, A.3
  • 38
    • 0142091718 scopus 로고    scopus 로고
    • Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase
    • Siegbahn P.E.M., Blomberg M.R.A., and Blomberg M.L. Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase. J. Phys. Chem., B 107 (2003) 10946-10955
    • (2003) J. Phys. Chem., B , vol.107 , pp. 10946-10955
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2    Blomberg, M.L.3
  • 39
    • 0035954401 scopus 로고    scopus 로고
    • Fast deuterium access to the buried magnesium/manganese site in cytochromecoxidase
    • Florens L., Schmidt B., McCracken J., and Ferguson-Miller S. Fast deuterium access to the buried magnesium/manganese site in cytochromecoxidase. Biochemistry 40 (2001) 7491-7497
    • (2001) Biochemistry , vol.40 , pp. 7491-7497
    • Florens, L.1    Schmidt, B.2    McCracken, J.3    Ferguson-Miller, S.4
  • 42
    • 0032318852 scopus 로고    scopus 로고
    • Proton uptake and release in cytochromecoxidase: separate pathways in time and space?
    • Mills D.A., and Ferguson-Miller S. Proton uptake and release in cytochromecoxidase: separate pathways in time and space?. Biochim. Biophys. Acta, Bioenerg. 1365 (1998) 46-52
    • (1998) Biochim. Biophys. Acta, Bioenerg. , vol.1365 , pp. 46-52
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 43
    • 0031036849 scopus 로고    scopus 로고
    • Aspartate-407 in Rhodobacter sphaeroides cytochromecoxidase is not required for proton pumping or manganese binding
    • Qian J., Shi W.J., Pressler M., Hoganson C., Mills D., Babcock G.T., and Ferguson-Miller S. Aspartate-407 in Rhodobacter sphaeroides cytochromecoxidase is not required for proton pumping or manganese binding. Biochemistry 36 (1997) 2539-2543
    • (1997) Biochemistry , vol.36 , pp. 2539-2543
    • Qian, J.1    Shi, W.J.2    Pressler, M.3    Hoganson, C.4    Mills, D.5    Babcock, G.T.6    Ferguson-Miller, S.7
  • 44
    • 0346103674 scopus 로고    scopus 로고
    • A discrete water exit pathway in the membrane protein cytochromecoxidase
    • Schmidt B., McCracken J., and Ferguson-Miller S. A discrete water exit pathway in the membrane protein cytochromecoxidase. PNAS 100 (2003) 15539-15542
    • (2003) PNAS , vol.100 , pp. 15539-15542
    • Schmidt, B.1    McCracken, J.2    Ferguson-Miller, S.3
  • 45
    • 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 J.W., Puustinen A., Alben J.O., Gennis R.B., 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 (1993) 10923-10928
    • (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
  • 47
    • 0028913025 scopus 로고
    • 3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135 → Asn
    • 3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135 → Asn. Biochemistry 34 (1995) 4428-44233
    • (1995) Biochemistry , vol.34 , pp. 4428-44233
    • García-Horsman, J.A.1    Puustinen, A.2    Gennis, R.B.3    Wikström, M.4
  • 48
    • 18744381863 scopus 로고    scopus 로고
    • Computer simulation of explicit proton translocation in cytochromecoxidase: the D-pathway
    • Xu J., and Voth G.A. Computer simulation of explicit proton translocation in cytochromecoxidase: the D-pathway. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 6795-6800
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6795-6800
    • Xu, J.1    Voth, G.A.2
  • 49
    • 0032311173 scopus 로고    scopus 로고
    • Structure and dynamics of a proton shuttle in cytochromecoxidase
    • Pomès R., Hummer G., and Wikström M. Structure and dynamics of a proton shuttle in cytochromecoxidase. Biochim. Biophys. Acta 1365 (1998) 255-260
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 255-260
    • Pomès, R.1    Hummer, G.2    Wikström, M.3
  • 50
    • 0031973948 scopus 로고    scopus 로고
    • Oxygen and proton pathways in cytochromecoxidase
    • Hofacker I., and Schulten K. Oxygen and proton pathways in cytochromecoxidase. Proteins 30 (1998) 100-107
    • (1998) Proteins , vol.30 , pp. 100-107
    • Hofacker, I.1    Schulten, K.2
  • 51
    • 0034663652 scopus 로고    scopus 로고
    • Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochromecoxidase
    • Ädelroth P., Karpefors M., Gilderson G., Tomson F.L., Gennis R.B., and Brzezinski P. Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochromecoxidase. Biochim. Biophys. Acta 1459 (2000) 533-539
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 533-539
    • Ädelroth, P.1    Karpefors, M.2    Gilderson, G.3    Tomson, F.L.4    Gennis, R.B.5    Brzezinski, P.6
  • 52
    • 13244260957 scopus 로고    scopus 로고
    • Thermodynamic properties of internal water molecules in the hydrophobic cavity around the catalytic center of cytochromecoxidase
    • Tashiro M., and Stuchebrukhov A.A. Thermodynamic properties of internal water molecules in the hydrophobic cavity around the catalytic center of cytochromecoxidase. J. Phys. Chem., B 109 (2005) 1015-1022
    • (2005) J. Phys. Chem., B , vol.109 , pp. 1015-1022
    • Tashiro, M.1    Stuchebrukhov, A.A.2
  • 57
    • 0037015164 scopus 로고    scopus 로고
    • The entry point of the K-proton-transfer pathway in cytochromecoxidase
    • Brändén M., Tomson F., Gennis R.B., and Brzezinski P. The entry point of the K-proton-transfer pathway in cytochromecoxidase. Biochemistry 41 (2002) 10794-10798
    • (2002) Biochemistry , vol.41 , pp. 10794-10798
    • Brändén, M.1    Tomson, F.2    Gennis, R.B.3    Brzezinski, P.4
  • 58
    • 7144257841 scopus 로고    scopus 로고
    • The role of electrostatic interactions for cytochromecoxidase function
    • Kannt A., Lancaster C.R., and Michel H. The role of electrostatic interactions for cytochromecoxidase function. J. Bioenerg. Biomembranes 30 (1998) 81-87
    • (1998) J. Bioenerg. Biomembranes , vol.30 , pp. 81-87
    • Kannt, A.1    Lancaster, C.R.2    Michel, H.3
  • 61
    • 11144304570 scopus 로고    scopus 로고
    • A molecular dynamics study of water chain formation in the proton-conducting K channel of cytochromecoxidase
    • Cukier R.I. A molecular dynamics study of water chain formation in the proton-conducting K channel of cytochromecoxidase. Biochim. Biophys. Acta 1706 (2005) 134-146
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 134-146
    • Cukier, R.I.1
  • 63
    • 0031745229 scopus 로고    scopus 로고
    • Crystal structure of bovine heart cytochromecoxidase at 2.8 A resolution
    • Yoshikawa S., Shinzawa-Itoh K., and Tsukihara T. Crystal structure of bovine heart cytochromecoxidase at 2.8 A resolution. J. Bioenerg. Biomembranes 30 (1998) 7-14
    • (1998) J. Bioenerg. Biomembranes , vol.30 , pp. 7-14
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Tsukihara, T.3
  • 65
    • 0034696637 scopus 로고    scopus 로고
    • Mutations in the putative H-channel in the cytochromecoxidase 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., and Gennis R.B. Mutations in the putative H-channel in the cytochromecoxidase 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
  • 66
    • 0031798637 scopus 로고    scopus 로고
    • Cytochromecoxidase (Heme aa(3)) from Paracoccus denitrificans: analysis of mutations in putative proton channels of subunit I
    • Pfitzner U., Odenwald A., Ostermann T., Weingard L., Ludwig B., and Richter O.M.H. Cytochromecoxidase (Heme aa(3)) from Paracoccus denitrificans: analysis of mutations in putative proton channels of subunit I. J. Bioenerg. Biomembranes 30 (1998) 89-97
    • (1998) J. Bioenerg. Biomembranes , vol.30 , pp. 89-97
    • Pfitzner, U.1    Odenwald, A.2    Ostermann, T.3    Weingard, L.4    Ludwig, B.5    Richter, O.M.H.6
  • 67
    • 23844453716 scopus 로고    scopus 로고
    • Is a third proton-conducting pathway operative in bacterial cytochromecoxidase?
    • Salje J., Ludwig B., and Richter O.M. Is a third proton-conducting pathway operative in bacterial cytochromecoxidase?. Biochem. Soc. Trans. 33 (2005) 829-831
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 829-831
    • Salje, J.1    Ludwig, B.2    Richter, O.M.3
  • 68
    • 0033539481 scopus 로고    scopus 로고
    • How oxygen is activated and reduced in respiration
    • Babcock G.T. How oxygen is activated and reduced in respiration. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 12971-12973
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12971-12973
    • Babcock, G.T.1
  • 70
    • 0037056048 scopus 로고    scopus 로고
    • Proton translocation by cytochromecoxidase in different phases of the catalytic cycle
    • Wikström M., and Verkhovsky M.I. Proton translocation by cytochromecoxidase in different phases of the catalytic cycle. Biochim. Biophys. Acta, Bioenerg. 1555 (2002) 128-132
    • (2002) Biochim. Biophys. Acta, Bioenerg. , vol.1555 , pp. 128-132
    • Wikström, M.1    Verkhovsky, M.I.2
  • 72
    • 1942472486 scopus 로고    scopus 로고
    • Cytochromecoxidase: 25 years of the elusive proton pump
    • Wikström M. Cytochromecoxidase: 25 years of the elusive proton pump. Biochim. Biophys. Acta 1655 (2004) 241-247
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 241-247
    • Wikström, M.1
  • 73
    • 0035912857 scopus 로고    scopus 로고
    • Charge translocation coupled to electron injection into oxidized cytochromecoxidase from Paracoccus denitrificans
    • Verkhovsky M.I., Tuukkanen A., Backgren C., Puustinen A., and Wikström M. Charge translocation coupled to electron injection into oxidized cytochromecoxidase from Paracoccus denitrificans. Biochemistry 40 (2001) 7077-7083
    • (2001) Biochemistry , vol.40 , pp. 7077-7083
    • Verkhovsky, M.I.1    Tuukkanen, A.2    Backgren, C.3    Puustinen, A.4    Wikström, M.5
  • 74
    • 1942472472 scopus 로고    scopus 로고
    • Time-resolved optical absorption studies of cytochrome oxidase dynamics
    • Einarsdóttir Ó., and Szundi I. Time-resolved optical absorption studies of cytochrome oxidase dynamics. Biochim. Biophys. Acta, Bioenerg. 1655 (2004) 263-273
    • (2004) Biochim. Biophys. Acta, Bioenerg. , vol.1655 , pp. 263-273
    • Einarsdóttir, Ó.1    Szundi, I.2
  • 76
    • 0029775911 scopus 로고    scopus 로고
    • Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochromecoxidase
    • Morgan J.E., Verkhovsky M.I., and Wikström M. Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochromecoxidase. Biochemistry 35 (1996) 12235-12240
    • (1996) Biochemistry , vol.35 , pp. 12235-12240
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 77
    • 0037173596 scopus 로고    scopus 로고
    • P(M) and P(R) forms of cytochromecoxidase have different spectral properties
    • Einarsdóttir Ó., Szundi I., Van Eps N., and Sucheta A. P(M) and P(R) forms of cytochromecoxidase have different spectral properties. J. Inorg. Biochem. 91 (2002) 87-93
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 87-93
    • Einarsdóttir, Ó.1    Szundi, I.2    Van Eps, N.3    Sucheta, A.4
  • 78
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochromecoxidase
    • Faxén K., Gilderson G., Ädelroth P., and Brzezinski P. A mechanistic principle for proton pumping by cytochromecoxidase. Nature 437 (2005) 286-289
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxén, K.1    Gilderson, G.2    Ädelroth, P.3    Brzezinski, P.4
  • 81
    • 0032487395 scopus 로고    scopus 로고
    • Factors determining electron-transfer rates in cytochromecoxidase: investigation of the oxygen reaction in the R. sphaeroides and bovine enzymes
    • Ädelroth P., Ek M., and Brzezinski P. Factors determining electron-transfer rates in cytochromecoxidase: investigation of the oxygen reaction in the R. sphaeroides and bovine enzymes. Biochim. Biophys. Acta 1367 (1998) 107-117
    • (1998) Biochim. Biophys. Acta , vol.1367 , pp. 107-117
    • Ädelroth, P.1    Ek, M.2    Brzezinski, P.3
  • 82
    • 0343580460 scopus 로고    scopus 로고
    • Glutamate 286 in cytochrome aa3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen
    • Ädelroth P., Svensson Ek M., Mitchell D.M., Gennis R.B., and Brzezinski P. Glutamate 286 in cytochrome aa3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen. Biochemistry 36 (1997) 13824-13829
    • (1997) Biochemistry , vol.36 , pp. 13824-13829
    • Ädelroth, P.1    Svensson Ek, M.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 83
    • 0031744648 scopus 로고    scopus 로고
    • Pathways of proton transfer in cytochromecoxidase
    • Brzezinski P., and Ädelroth P. Pathways of proton transfer in cytochromecoxidase. J. Bioenerg. Biomembranes 30 (1998) 99-107
    • (1998) J. Bioenerg. Biomembranes , vol.30 , pp. 99-107
    • Brzezinski, P.1    Ädelroth, P.2
  • 84
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochromecoxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • Konstantinov A.A., Siletsky S., Mitchell D., Kaulen A., and Gennis R.B. The roles of the two proton input channels in cytochromecoxidase 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 (1997) 9085-9090
    • (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
  • 85
    • 0032478132 scopus 로고    scopus 로고
    • Mechanism of inhibition of electron transfer by amino acid replacement K362M in a proton channel of Rhodobacter sphaeroides cytochromecoxidase
    • Vygodina T.V., Pecoraro C., Mitchell D., Gennis R., and Konstantinov A.A. Mechanism of inhibition of electron transfer by amino acid replacement K362M in a proton channel of Rhodobacter sphaeroides cytochromecoxidase. Biochemistry 37 (1998) 3053-3061
    • (1998) Biochemistry , vol.37 , pp. 3053-3061
    • Vygodina, T.V.1    Pecoraro, C.2    Mitchell, D.3    Gennis, R.4    Konstantinov, A.A.5
  • 86
    • 0034712938 scopus 로고    scopus 로고
    • Single-electron reduction of the oxidized state is coupled to proton uptake via the K pathway in Paracoccus denitrificans cytochromecoxidase
    • 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 cytochromecoxidase. 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
  • 87
    • 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 M.I. The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases. Biochim. Biophys. Acta 1459 (2000) 514-520
    • (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
  • 88
    • 0033264078 scopus 로고    scopus 로고
    • The deuterium isotope effect as a tool to investigate enzyme catalysis: proton-transfer control mechanisms in cytochromecoxidase
    • Karpefors M., Ädelroth P., Aagaard A., Smirnova I.A., and Brzezinski P. The deuterium isotope effect as a tool to investigate enzyme catalysis: proton-transfer control mechanisms in cytochromecoxidase. Isr. J. Chem. 39 (1999) 427-437
    • (1999) Isr. J. Chem. , vol.39 , pp. 427-437
    • Karpefors, M.1    Ädelroth, P.2    Aagaard, A.3    Smirnova, I.A.4    Brzezinski, P.5
  • 89
    • 0034643829 scopus 로고    scopus 로고
    • Localized control of proton transfer through the D-pathway in cytochromecoxidase: application of the proton-inventory technique
    • Karpefors M., Ädelroth P., and Brzezinski P. Localized control of proton transfer through the D-pathway in cytochromecoxidase: application of the proton-inventory technique. Biochemistry 39 (2000) 6850-6856
    • (2000) Biochemistry , vol.39 , pp. 6850-6856
    • Karpefors, M.1    Ädelroth, P.2    Brzezinski, P.3
  • 90
    • 0032555160 scopus 로고    scopus 로고
    • The proton collecting function of the inner surface of cytochromecoxidase from Rhodobacter sphaeroides
    • Marantz Y., Nachliel E., Aagaard A., Brzezinski P., and Gutman M. The proton collecting function of the inner surface of cytochromecoxidase from Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 8590-8595
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 8590-8595
    • Marantz, Y.1    Nachliel, E.2    Aagaard, A.3    Brzezinski, P.4    Gutman, M.5
  • 91
    • 0030665489 scopus 로고    scopus 로고
    • Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin
    • Checover S., Nachliel E., Dencher N.A., and Gutman M. Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin. Biochemistry 36 (1997) 13919-13928
    • (1997) Biochemistry , vol.36 , pp. 13919-13928
    • Checover, S.1    Nachliel, E.2    Dencher, N.A.3    Gutman, M.4
  • 92
    • 0035909798 scopus 로고    scopus 로고
    • Proton-collecting properties of bovine heart cytochromecoxidase: kinetic and electrostatic analysis
    • Marantz Y., Einarsdóttir O., Nachliel E., and Gutman M. Proton-collecting properties of bovine heart cytochromecoxidase: kinetic and electrostatic analysis. Biochemistry 40 (2001) 15086-15097
    • (2001) Biochemistry , vol.40 , pp. 15086-15097
    • Marantz, Y.1    Einarsdóttir, O.2    Nachliel, E.3    Gutman, M.4
  • 94
    • 29244472486 scopus 로고    scopus 로고
    • An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochromecoxidase from Paracoccus denitrificans
    • Ribacka C., Verkhovsky M.I., Belevich I., Bloch D.A., Puustinen A., and Wikström M. An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochromecoxidase from Paracoccus denitrificans. Biochemistry 44 (2005) 16502-16512
    • (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
  • 96
    • 0024408677 scopus 로고
    • The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochromecoxidase with dioxygen
    • Oliveberg M., Brzezinski P., and Malmström B.G. The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochromecoxidase with dioxygen. Biochim. Biophys. Acta 977 (1989) 322-328
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 322-328
    • Oliveberg, M.1    Brzezinski, P.2    Malmström, B.G.3
  • 97
    • 0037133031 scopus 로고    scopus 로고
    • Mutants of the Cu-A site in cytochromecoxidase of Rhodobacter sphaeroides: I. Spectral and functional properties
    • Zhen Y.J., Schmidt B., Kang U.G., Antholine W., and Ferguson-Miller S. Mutants of the Cu-A site in cytochromecoxidase of Rhodobacter sphaeroides: I. Spectral and functional properties. Biochemistry 41 (2002) 2288-2297
    • (2002) Biochemistry , vol.41 , pp. 2288-2297
    • Zhen, Y.J.1    Schmidt, B.2    Kang, U.G.3    Antholine, W.4    Ferguson-Miller, S.5
  • 99
    • 0032552970 scopus 로고    scopus 로고
    • Single electron reduction of cytochromecoxidase compound F: resolution of partial steps by transient spectroscopy
    • Zaslavsky D., Sadoski R.C., Wang K.F., Durham B., Gennis R.B., and Millett F. Single electron reduction of cytochromecoxidase compound F: resolution of partial steps by transient spectroscopy. Biochemistry 37 (1998) 14910-14916
    • (1998) Biochemistry , vol.37 , pp. 14910-14916
    • Zaslavsky, D.1    Sadoski, R.C.2    Wang, K.F.3    Durham, B.4    Gennis, R.B.5    Millett, F.6
  • 100
    • 0033602933 scopus 로고    scopus 로고
    • Aspartate-132 in cytochromecoxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation
    • Smirnova I.A., Ädelroth P., Gennis R.B., and Brzezinski P. Aspartate-132 in cytochromecoxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation. Biochemistry 38 (1999) 6826-6833
    • (1999) Biochemistry , vol.38 , pp. 6826-6833
    • Smirnova, I.A.1    Ädelroth, P.2    Gennis, R.B.3    Brzezinski, P.4
  • 102
    • 0035823541 scopus 로고    scopus 로고
    • Exposure of bovine cytochromecoxidase to high triton X-100 or to alkaline conditions causes a dramatic change in the rate of reduction of compound F
    • Sadoski R.C., Zaslavsky D., Gennis R.B., Durham B., and Millett F. Exposure of bovine cytochromecoxidase to high triton X-100 or to alkaline conditions causes a dramatic change in the rate of reduction of compound F. J. Biol. Chem. 276 (2001) 33616-33620
    • (2001) J. Biol. Chem. , vol.276 , pp. 33616-33620
    • Sadoski, R.C.1    Zaslavsky, D.2    Gennis, R.B.3    Durham, B.4    Millett, F.5
  • 103
    • 0028855258 scopus 로고
    • Rapid kinetics of membrane potential generation by cytochromecoxidase with the photoactive Ru(II)-tris-bipyridyl derivative of cytochromecas electron donor
    • Zaslavsky D.L., Smirnova I.A., Siletsky S.A., Kaulen A.D., Millett F., and Konstantinov A.A. Rapid kinetics of membrane potential generation by cytochromecoxidase with the photoactive Ru(II)-tris-bipyridyl derivative of cytochromecas 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
  • 104
    • 10644252589 scopus 로고    scopus 로고
    • Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochromecoxidase
    • Siletsky S.A., Pawate A.S., Weiss K., Gennis R.B., and Konstantinov A.A. Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochromecoxidase. J. Biol. Chem. 279 (2004) 52558-52565
    • (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
  • 105
    • 0037452497 scopus 로고    scopus 로고
    • Intramolecular proton-transfer reactions in a membrane-bound proton pump: the effect of pH on the peroxy to ferryl transition in cytochromecoxidase
    • Namslauer A., Aagaard A., Katsonouri A., and Brzezinski P. Intramolecular proton-transfer reactions in a membrane-bound proton pump: the effect of pH on the peroxy to ferryl transition in cytochromecoxidase. Biochemsitry 42 (2003) 1488-1498
    • (2003) Biochemsitry , vol.42 , pp. 1488-1498
    • Namslauer, A.1    Aagaard, A.2    Katsonouri, A.3    Brzezinski, P.4
  • 106
    • 0038408885 scopus 로고    scopus 로고
    • Subunit III of cytochromecoxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH
    • Gilderson G., Salomonsson L., Aagaard A., Gray J., Brzezinski P., and Hosler J. Subunit III of cytochromecoxidase of Rhodobacter sphaeroides is required to maintain rapid proton uptake through the D pathway at physiologic pH. Biochemistry 42 (2003) 7400-7409
    • (2003) Biochemistry , vol.42 , pp. 7400-7409
    • Gilderson, G.1    Salomonsson, L.2    Aagaard, A.3    Gray, J.4    Brzezinski, P.5    Hosler, J.6
  • 107
    • 0028925948 scopus 로고
    • Internal electron transfer in cytochromecoxidase from Rhodobacter sphaeroides
    • Ädelroth P., Brzezinski P., and Malmström B.G. Internal electron transfer in cytochromecoxidase from Rhodobacter sphaeroides. Biochemistry 34 (1995) 2844-2849
    • (1995) Biochemistry , vol.34 , pp. 2844-2849
    • Ädelroth, P.1    Brzezinski, P.2    Malmström, B.G.3
  • 108
    • 0030573678 scopus 로고    scopus 로고
    • 'As prepared' forms of fully oxidised haem/Cu terminal oxidases
    • Moody A.J. 'As prepared' forms of fully oxidised haem/Cu terminal oxidases. Biochim. Biophys. Acta 1276 (1996) 6-20
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 6-20
    • Moody, A.J.1
  • 110
    • 0037007627 scopus 로고    scopus 로고
    • Reduction of cytochromecoxidase by a second electron leads to proton translocation
    • Ruitenberg M., Kannt A., Bamberg E., Fendler K., and Michel H. Reduction of cytochromecoxidase 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
  • 111
    • 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
  • 112
    • 30144445932 scopus 로고    scopus 로고
    • Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
    • Garczarek F., and Gerwert K. Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy. Nature 439 (2006) 109-112
    • (2006) Nature , vol.439 , pp. 109-112
    • Garczarek, F.1    Gerwert, K.2


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