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Volumn 1777, Issue 3, 2008, Pages 277-284

Electrostatic control of proton pumping in cytochrome c oxidase

Author keywords

Binuclear center; Continuum electrostatics; Cytochrome c oxidase; Proton pumping mechanism; Redox coupled proton transport; Vectorial proton transport

Indexed keywords

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

EID: 39949085428     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.11.010     Document Type: Article
Times cited : (44)

References (47)
  • 1
    • 33748885262 scopus 로고    scopus 로고
    • Towards the mechanism of proton pumping by the haem-copper oxidases
    • Wikström M., and Verkhovsky M.I. Towards the mechanism of proton pumping by the haem-copper oxidases. Biochim. Biophys. Acta 1757 (2006) 1047-1051
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1047-1051
    • Wikström, M.1    Verkhovsky, M.I.2
  • 2
    • 33749137961 scopus 로고    scopus 로고
    • Transmembrane proton translocation by cytochrome c oxidase
    • Brändén G., Gennis R.B., and Brzezinski P. Transmembrane proton translocation by cytochrome c oxidase. Biochim. Biophys. Acta 1757 (2006) 1052-1063
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1052-1063
    • Brändén, G.1    Gennis, R.B.2    Brzezinski, P.3
  • 3
    • 33746601087 scopus 로고    scopus 로고
    • Design principles of proton-pumping haem-copper oxidases
    • Brzezinski P., and Älderoth P. Design principles of proton-pumping haem-copper oxidases. Curr. Opin. Struct. Biol. 16 (2006) 465-472
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 465-472
    • Brzezinski, P.1    Älderoth, P.2
  • 4
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • Wikström M. Proton pump coupled to cytochrome c oxidase in mitochondria. Nature 266 (1977) 271-273
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.1
  • 5
    • 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 A.A., Siletsky S., Mitchell D., Kaulen A., and Gennis R.B. 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 (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
  • 6
    • 0031744648 scopus 로고    scopus 로고
    • Pathways of proton transfer in cytochrome c oxidase
    • Brzezinski P., and Älderoth P. Pathways of proton transfer in cytochrome c oxidase. J. Bioenerg. Biomembranes 30 (1998) 99-107
    • (1998) J. Bioenerg. Biomembranes , vol.30 , pp. 99-107
    • Brzezinski, P.1    Älderoth, P.2
  • 8
    • 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 (1998) 12819-12824
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12819-12824
    • Michel, H.1
  • 10
    • 23244450116 scopus 로고    scopus 로고
    • Water chain formation and possible proton pumping routes in Rhodobacter sphaeroides cytochrome c oxidase: a molecular dynamics comparison of the wild type and R481K mutant
    • Seibold S.A., Mills D.A., Ferguson-Miller S., and Cuckier R.I. Water chain formation and possible proton pumping routes in Rhodobacter sphaeroides cytochrome c oxidase: a molecular dynamics comparison of the wild type and R481K mutant. Biochemistry 44 (2005) 10475-10485
    • (2005) Biochemistry , vol.44 , pp. 10475-10485
    • Seibold, S.A.1    Mills, D.A.2    Ferguson-Miller, S.3    Cuckier, R.I.4
  • 11
    • 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
  • 12
    • 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
  • 13
    • 33748481558 scopus 로고    scopus 로고
    • Structural and chemical changes of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase revealed by IR spectroscopy with labeled tyrosines and histidine
    • Iwaki M., Puustinen A., Wikström M., and Rich P.R. Structural and chemical changes of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase revealed by IR spectroscopy with labeled tyrosines and histidine. Biochemistry 45 (2006) 10873-10885
    • (2006) Biochemistry , vol.45 , pp. 10873-10885
    • Iwaki, M.1    Puustinen, A.2    Wikström, M.3    Rich, P.R.4
  • 17
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxén K., Gilderson G., Älderoth 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
    • Faxén, K.1    Gilderson, G.2    Älderoth, P.3    Brzezinski, P.4
  • 18
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • Belevich I., Verkhovsky M.I., and Wikström M. Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase. Nature 440 (2006) 829-832
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikström, M.3
  • 19
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • Wikström M., and Verkhovsky M.I. Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases. Biochim. Biophys. Acta 1767 (2007) 1200-1214
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1200-1214
    • Wikström, M.1    Verkhovsky, M.I.2
  • 20
    • 1942472486 scopus 로고    scopus 로고
    • Cytochrome c oxidase: 25 years of the elusive proton pump
    • Wikström M. Cytochrome c oxidase: 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
  • 22
    • 33745602474 scopus 로고    scopus 로고
    • Elementary steps of proton translocation in the catalytic cycle of cytochrome c oxidase
    • Verkhovsky M.I., Belevich I., Bloch D., and Wikström M. Elementary steps of proton translocation in the catalytic cycle of cytochrome c oxidase. Biochim. Biophys. Acta 1757 (2006) 401-407
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 401-407
    • Verkhovsky, M.I.1    Belevich, I.2    Bloch, D.3    Wikström, M.4
  • 23
    • 0034711407 scopus 로고    scopus 로고
    • Oxygen activation and reduction in respiration: involvement of redox-active tyrosine
    • 244
    • Proshlyakov D.A., Pressler M.A., DeMaso C., Leykam J.F., DeWitt D.L., and Babcock G.T. Oxygen activation and reduction in respiration: involvement of redox-active tyrosine. 244. Science 290 (2000) 1588-1591
    • (2000) Science , vol.290 , pp. 1588-1591
    • Proshlyakov, D.A.1    Pressler, M.A.2    DeMaso, C.3    Leykam, J.F.4    DeWitt, D.L.5    Babcock, G.T.6
  • 24
    • 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
  • 26
    • 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
  • 27
    • 0346734127 scopus 로고    scopus 로고
    • Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase
    • Namslauer A., Pawate A.S., Gennis R.B., and Brzezinski P. Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 15543-15547
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15543-15547
    • Namslauer, A.1    Pawate, A.S.2    Gennis, R.B.3    Brzezinski, P.4
  • 29
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase
    • Kannt A.C., Lancaster R.D., and Michel H. The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase. Biophys. J. 74 (1998) 708-721
    • (1998) Biophys. J. , vol.74 , pp. 708-721
    • Kannt, A.C.1    Lancaster, R.D.2    Michel, H.3
  • 32
    • 0037069405 scopus 로고    scopus 로고
    • A mutation in subunit I of cytochrome c oxidase from Rhodobacter sphaeroides results in an increase in steady state activity but completely eliminates proton pumping
    • Pawate A.S., Morgan J., Namslauer A., Mills D., Brzezinski P., Ferguson-Miller S., and Gennis R.B. A mutation in subunit I of cytochrome c oxidase from Rhodobacter sphaeroides results in an increase in steady state activity but completely eliminates proton pumping. Biochemistry 41 (2002) 13417-13423
    • (2002) Biochemistry , vol.41 , pp. 13417-13423
    • Pawate, A.S.1    Morgan, J.2    Namslauer, A.3    Mills, D.4    Brzezinski, P.5    Ferguson-Miller, S.6    Gennis, R.B.7
  • 33
    • 25444491194 scopus 로고    scopus 로고
    • 3-type cytochrome c oxidase from Rhodobacter sphaeroides
    • 3-type cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 44 (2005) 12767-12774
    • (2005) Biochemistry , vol.44 , pp. 12767-12774
    • Han, D.1    Morgan, J.E.2    Gennis, R.B.3
  • 34
    • 25844460787 scopus 로고    scopus 로고
    • Titration behavior of residues at the entrance of the D-pathway of cytochrome c oxidase from Paracoccus denitrificans investigated by continuum electrostatic calculations
    • Olkhova E., Helms V., and Michel H. Titration behavior of residues at the entrance of the D-pathway of cytochrome c oxidase from Paracoccus denitrificans investigated by continuum electrostatic calculations. Biophys. J. 89 (2005) 2324-2331
    • (2005) Biophys. J. , vol.89 , pp. 2324-2331
    • Olkhova, E.1    Helms, V.2    Michel, H.3
  • 35
    • 34548170174 scopus 로고    scopus 로고
    • Energy diagrams and mechanisms for proton pumping in cytochrome c oxidase
    • Siegbahn P.E.M., and Blomberg M.R.A. Energy diagrams and mechanisms for proton pumping in cytochrome c oxidase. Biochim. Biophys. Acta 1767 (2007) 1143-1156
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1143-1156
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 36
    • 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., Törnroth 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 (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
  • 38
    • 33751157732 scopus 로고
    • Ab Initio calculations of vibrational absorption and circular dichroism spectra using SCF, MP2, and density functional theory force fields
    • Stevens P.J., Devlin J.F., Chabalowski C.F., and Frisch M.J. Ab Initio calculations of vibrational absorption and circular dichroism spectra using SCF, MP2, and density functional theory force fields. J. Phys. Chem. 98 (1994) 11623
    • (1994) J. Phys. Chem. , vol.98 , pp. 11623
    • Stevens, P.J.1    Devlin, J.F.2    Chabalowski, C.F.3    Frisch, M.J.4
  • 39
    • 0005744966 scopus 로고
    • Compact effective potentials and efficient shared-exponent basis sets for the first- and second-row atoms
    • Stevens W.J., Bash H., and Krauss M. Compact effective potentials and efficient shared-exponent basis sets for the first- and second-row atoms. J. Chem. Phys. 81 (1984) 6026
    • (1984) J. Chem. Phys. , vol.81 , pp. 6026
    • Stevens, W.J.1    Bash, H.2    Krauss, M.3
  • 40
    • 0001510524 scopus 로고
    • Relativistic compact effective potentials and efficient, shared-exponent basis sets for the third-, fourth-, and fifth-row atoms
    • Stevens W.J., Krauss M., Bash H., and Jasien P.G. Relativistic compact effective potentials and efficient, shared-exponent basis sets for the third-, fourth-, and fifth-row atoms. Can. J. Chem. 70 (1992) 612
    • (1992) Can. J. Chem. , vol.70 , pp. 612
    • Stevens, W.J.1    Krauss, M.2    Bash, H.3    Jasien, P.G.4
  • 43
    • 29144445121 scopus 로고    scopus 로고
    • Acidity of a Cu-bound histidine in the binuclear center of cytochrome c oxidase
    • Fadda E., Chakrabarti N., and Pomès R. Acidity of a Cu-bound histidine in the binuclear center of cytochrome c oxidase. J. Phys. Chem., B 109 (2005) 22629-22640
    • (2005) J. Phys. Chem., B , vol.109 , pp. 22629-22640
    • Fadda, E.1    Chakrabarti, N.2    Pomès, R.3
  • 44
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model electrostatic forces from numerical solutions to the Poisson Boltzmann equation
    • Im W., Beglov D., and Roux B. Continuum solvation model electrostatic forces from numerical solutions to the Poisson Boltzmann equation. Comp. Phys. Comm. 111 (1998) 59-75
    • (1998) Comp. Phys. Comm. , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2    Roux, B.3
  • 46
    • 0032968444 scopus 로고    scopus 로고
    • Optimized atomic radii for protein continuum electrostatic solvation forces
    • Nina M., Im W., and Roux B. Optimized atomic radii for protein continuum electrostatic solvation forces. Biophys. Chem. 78 (1999) 89-96
    • (1999) Biophys. Chem. , vol.78 , pp. 89-96
    • Nina, M.1    Im, W.2    Roux, B.3
  • 47
    • 0037056048 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase in different phases of the catalytic cycle
    • Wikström M., and Verkhovsky M.I. Proton translocation by cytochrome c oxidase 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


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