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Volumn 6, Issue 4, 1996, Pages 460-466

Cytochrome c oxidase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME C OXIDASE; MEMBRANE PROTEIN; PROTON PUMP;

EID: 0030220806     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80110-2     Document Type: Article
Times cited : (85)

References (49)
  • 1
    • 0001022291 scopus 로고
    • Über Eisen, den sauerstoffübertragenden Bestandteil des Atmungsfermentes
    • Warburg O. Über Eisen, den sauerstoffübertragenden Bestandteil des Atmungsfermentes. Biochem Z. 152:1924;479-494.
    • (1924) Biochem Z , vol.152 , pp. 479-494
    • Warburg, O.1
  • 2
    • 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. 98:1925;312-339.
    • (1925) Proc R Soc Lond B Biol Sci , vol.98 , pp. 312-339
    • Keilin, D.1
  • 3
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • v fragment. Mechanisms for the function of this redox-linked proton pump are discussed.
    • v fragment. Mechanisms for the function of this redox-linked proton pump are discussed.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 4
    • 0029652024 scopus 로고
    • Structure of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å
    • of outstanding interest. The structure of the cofactors and metal centers of the mitochondrial COX from bovine heart is described at 2.8 Å resolution.
    • of outstanding interest Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S. Structure of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å Science. 269:1995;1069-1074 The structure of the cofactors and metal centers of the mitochondrial COX from bovine heart is described at 2.8 Å resolution.
    • (1995) Science , vol.269 , pp. 1069-1074
    • Tsukihara, T.1    Aoyama, H.2    Yamashita, E.3    Tomizaki, T.4    Yamaguchi, H.5    Shinzawa-Itoh, K.6    Nakashima, R.7    Yaono, R.8    Yoshikawa, S.9
  • 6
    • 0028137093 scopus 로고
    • The cytochrome oxidase superfamily of redox-driven proton pumps
    • Calhoun MW, Thomas JW, Gennis RB. The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem Sci. 19:1994;325-330.
    • (1994) Trends Biochem Sci , vol.19 , pp. 325-330
    • Calhoun, M.W.1    Thomas, J.W.2    Gennis, R.B.3
  • 7
    • 0027993918 scopus 로고
    • Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase
    • Hill BC. Modeling the sequence of electron transfer reactions in the single turnover of reduced, mammalian cytochrome c oxidase. J Biol Chem. 269:1994;2419-2425.
    • (1994) J Biol Chem , vol.269 , pp. 2419-2425
    • Hill, B.C.1
  • 8
    • 0029558330 scopus 로고
    • Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center
    • of special interest. The crystal structures of the periplasmic fragment from the wild-type subunit II of E. coli quinol oxidase and from a mutant with an engineered dinuclear copper center are described at resolutions of 2.5 and 2.3 Å, respectively.
    • of special interest Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center. Proc Natl Acad Sci USA. 92:1995;11955-11959 The crystal structures of the periplasmic fragment from the wild-type subunit II of E. coli quinol oxidase and from a mutant with an engineered dinuclear copper center are described at resolutions of 2.5 and 2.3 Å, respectively.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11955-11959
    • Wilmanns, M.1    Lappalainen, P.2    Kelly, M.3    Sauer-Eriksson, E.4    Saraste, M.5
  • 9
    • 0029556849 scopus 로고
    • Crystals and structures of cytochrome c oxidases - The end of an arduous road
    • Beinert H. Crystals and structures of cytochrome c oxidases - the end of an arduous road. Chem Biol. 2:1995;781-785.
    • (1995) Chem Biol , vol.2 , pp. 781-785
    • Beinert, H.1
  • 11
    • 0029681875 scopus 로고    scopus 로고
    • Protein structure: Proton-pumping oxidases
    • Gennis RB, Ferguson-Miller S. Protein structure: proton-pumping oxidases. Curr Biol. 6:1996;36-38.
    • (1996) Curr Biol , vol.6 , pp. 36-38
    • Gennis, R.B.1    Ferguson-Miller, S.2
  • 12
    • 0029645576 scopus 로고
    • Functional significance of cytochrome c oxidase structure
    • Scott RA. Functional significance of cytochrome c oxidase structure. Structure. 3:1995;981-986.
    • (1995) Structure , vol.3 , pp. 981-986
    • Scott, R.A.1
  • 13
    • 0025640889 scopus 로고
    • Structural features of cytochrome oxidase
    • Saraste M. Structural features of cytochrome oxidase. Q Rev Biophys. 23:1990;331-366.
    • (1990) Q Rev Biophys , vol.23 , pp. 331-366
    • Saraste, M.1
  • 14
    • 0028909685 scopus 로고
    • Structure and function of a molecular machine: Cytochrome c oxidase
    • Malatesta F, Antonini G, Sarti P, Brunori M. Structure and function of a molecular machine: cytochrome c oxidase. Biophys Chem. 54:1995;1-33.
    • (1995) Biophys Chem , vol.54 , pp. 1-33
    • Malatesta, F.1    Antonini, G.2    Sarti, P.3    Brunori, M.4
  • 15
    • 0028991525 scopus 로고
    • v fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase
    • of outstanding interest. The novel approach of co-crystallizing membrane proteins with antibody fragments leads to well diffracting three-dimensional crystals of the multisubunit membrane protein COX from Paracoccus denitrificans. Analysis of the crystal packing reveals that the polar contacts mediated by the antibody fragment are responsible for forming the well ordered crystal lattice.
    • v fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nature Struct Biol. 2:1995;842-846 The novel approach of co-crystallizing membrane proteins with antibody fragments leads to well diffracting three-dimensional crystals of the multisubunit membrane protein COX from Paracoccus denitrificans. Analysis of the crystal packing reveals that the polar contacts mediated by the antibody fragment are responsible for forming the well ordered crystal lattice.
    • (1995) Nature Struct Biol , vol.2 , pp. 842-846
    • Ostermeier, C.1    Iwata, S.2    Ludwig, B.3    Michel, H.4
  • 16
    • 0028798287 scopus 로고
    • Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes
    • v fragment, this technique provides the big advantage of very mild elution conditions.
    • v fragment, this technique provides the big advantage of very mild elution conditions.
    • (1995) Biotechnology , vol.13 , pp. 155-160
    • Kleymann, G.1    Ostermeier, C.2    Ludwig, B.3    Skerra, A.4    Michel, H.5
  • 19
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans
    • Haltia T, Semo N, Arrondo JLR, Goñi FM, Freire E. Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry. 33:1994;9731-9740.
    • (1994) Biochemistry , vol.33 , pp. 9731-9740
    • Haltia, T.1    Semo, N.2    Arrondo, J.L.R.3    Goñi, F.M.4    Freire, E.5
  • 20
    • 0028239826 scopus 로고
    • Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
    • Castresana J, Lübben M, Saraste M, Higgins DG. Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J. 13:1994;2516-2525.
    • (1994) EMBO J , vol.13 , pp. 2516-2525
    • Castresana, J.1    Lübben, M.2    Saraste, M.3    Higgins, D.G.4
  • 21
    • 0027169894 scopus 로고
    • Genetic fusion of subunits I, II, and III of the cytochrome bo ubiquinol oxidase from Escherichia coli results in a fully assembled and active enzyme
    • Ma J, Lemieux L, Gennis RB. Genetic fusion of subunits I, II, and III of the cytochrome bo ubiquinol oxidase from Escherichia coli results in a fully assembled and active enzyme. Biochemistry. 32:1993;7692-7697.
    • (1993) Biochemistry , vol.32 , pp. 7692-7697
    • Ma, J.1    Lemieux, L.2    Gennis, R.B.3
  • 23
    • 0028786047 scopus 로고
    • Evolution of energetic metabolism: The respiration-early hypothesis
    • of special interest. This paper presents evidence that aerobic respiration has a single origin and may have evolved before oxygen was released to the atmosphere by photosynthetic organisms.
    • of special interest Castresana J, Saraste M. Evolution of energetic metabolism: the respiration-early hypothesis. Trends Biochem Sci. 20:1995;443-448 This paper presents evidence that aerobic respiration has a single origin and may have evolved before oxygen was released to the atmosphere by photosynthetic organisms.
    • (1995) Trends Biochem Sci , vol.20 , pp. 443-448
    • Castresana, J.1    Saraste, M.2
  • 24
    • 0000914066 scopus 로고    scopus 로고
    • Metal-center assembly at the bacterial multicopper enzyme nitrous oxide reductase
    • Zumft WC, Kroneck PMH. Metal-center assembly at the bacterial multicopper enzyme nitrous oxide reductase. Adv Inorg Biochem. 11:1996;193-221.
    • (1996) Adv Inorg Biochem , vol.11 , pp. 193-221
    • Zumft, W.C.1    Kroneck, P.M.H.2
  • 29
    • 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, 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. 34:1995;7586-7592.
    • (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
  • 30
    • 0029892297 scopus 로고    scopus 로고
    • Kinetic trapping of oxygen in cell respiration
    • of special interest. It is essential that the respiratory system has a high affinity for oxygen, but the binding of oxygen to the heme-copper oxidases is very weak. This paradox is solved by kinetic trapping of oxygen bound to the binuclear center. It is shown that fast electron transfer from the low-spin heme to the binuclear center is essential for this trapping.
    • of special interest Verkhovsky MI, Morgan JE, Puustinen A, Wikström M. Kinetic trapping of oxygen in cell respiration. Nature. 380:1996;268-270 It is essential that the respiratory system has a high affinity for oxygen, but the binding of oxygen to the heme-copper oxidases is very weak. This paradox is solved by kinetic trapping of oxygen bound to the binuclear center. It is shown that fast electron transfer from the low-spin heme to the binuclear center is essential for this trapping.
    • (1996) Nature , vol.380 , pp. 268-270
    • Verkhovsky, M.I.1    Morgan, J.E.2    Puustinen, A.3    Wikström, M.4
  • 31
    • 0028872508 scopus 로고
    • B promotes both binding and reduction of dioxygen at the heme-copper binuclear center in the Escherichia coli bo-type ubiquinol oxidase
    • B promotes both binding and reduction of dioxygen at the heme-copper binuclear center in the Escherichia coli bo-type ubiquinol oxidase. FEBS Lett. 370:1995;259-263.
    • (1995) FEBS Lett , vol.370 , pp. 259-263
    • Mogi, T.1    Hirano, T.2    Nakamura, H.3    Anraku, Y.4    Orii, Y.5
  • 32
    • 0029645280 scopus 로고
    • 3-type quinol oxidase from Bacillus subtilis: An ENDOR and EXAFS study
    • B site has a low symmetry, tetragonal coordination with two or three histidine nitrogens and one oxygen as ligands. The oxygenous copper ligand seems to possess an exchangeable proton.
    • B site has a low symmetry, tetragonal coordination with two or three histidine nitrogens and one oxygen as ligands. The oxygenous copper ligand seems to possess an exchangeable proton.
    • (1995) Biochemistry , vol.34 , pp. 10245-10255
    • Fann, Y.C.1    Ahmed, I.2    Blackburn, N.J.3    Boswell, J.S.4    Verkhovskaya, M.L.5    Hoffman, B.M.6    Wikström, M.7
  • 34
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock GT, Wikström M. Oxygen activation and the conservation of energy in cell respiration. Nature. 356:1992;301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 35
    • 0028219639 scopus 로고
    • Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site
    • Hallén S, Brzezinski P, Malmström BG. Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site. Biochemistry. 33:1994;1467-1472.
    • (1994) Biochemistry , vol.33 , pp. 1467-1472
    • Hallén, S.1    Brzezinski, P.2    Malmström, B.G.3
  • 36
    • 0029036305 scopus 로고
    • Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons
    • Verkhovsky MI, Morgan JE, Wikström M. Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: a role for protons. Biochemistry. 34:1995;7483-7491.
    • (1995) Biochemistry , vol.34 , pp. 7483-7491
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 37
    • 0028955899 scopus 로고
    • Fast reactions of cytochrome oxidase
    • Einarsdöttir Ó. Fast reactions of cytochrome oxidase. Biochim Biophys Acta. 1229:1995;129-147.
    • (1995) Biochim Biophys Acta , vol.1229 , pp. 129-147
    • Einarsdöttir Ó1
  • 38
    • 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. 338:1989;776-778.
    • (1989) Nature , vol.338 , pp. 776-778
    • Wikström, M.1
  • 39
    • 0028241769 scopus 로고
    • Proton uptake by cytochrome c oxidase on reduction and on ligand binding
    • Mitchell R, Rich PR. Proton uptake by cytochrome c oxidase on reduction and on ligand binding. Biochim Biophys Acta. 1186:1994;19-26.
    • (1994) Biochim Biophys Acta , vol.1186 , pp. 19-26
    • Mitchell, R.1    Rich, P.R.2
  • 40
    • 0028813330 scopus 로고
    • Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases
    • B-center is presented. Charge compensation can only be provided by protonation/deprotonation reactions.
    • B-center is presented. Charge compensation can only be provided by protonation/deprotonation reactions.
    • (1995) Aust J Plant Physiol , vol.22 , pp. 479-486
    • Rich, P.R.1
  • 41
    • 0029054720 scopus 로고
    • Understanding the cytochrome c oxidase proton pump: Thermodynamics of redox linkage
    • Musser SM, Chan SI. Understanding the cytochrome c oxidase proton pump: thermodynamics of redox linkage. Biophys J. 68:1995;2543-2555.
    • (1995) Biophys J , vol.68 , pp. 2543-2555
    • Musser, S.M.1    Chan, S.I.2
  • 42
    • 0028964820 scopus 로고
    • Intramolecular electron transfer and conformational changes in cytochrome c oxidase
    • Einarsdóttir Ó, Geogiadis KE, Sucheta A. Intramolecular electron transfer and conformational changes in cytochrome c oxidase. Biochemistry. 34:1995;496-508.
    • (1995) Biochemistry , vol.34 , pp. 496-508
    • Einarsdóttir Ó1    Geogiadis, K.E.2    Sucheta, A.3
  • 43
    • 0028607633 scopus 로고
    • The histidine cycle: A new model for proton translocation in the respiratory heme-copper oxidases
    • Morgan JE, Verkhovsky MI, Wikström M. The histidine cycle: a new model for proton translocation in the respiratory heme-copper oxidases. J Bioenerg Biomembr. 26:1994;599-608.
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 599-608
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 44
    • 0027380681 scopus 로고
    • o ubiquinol oxidase from Escherichia coli. An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center
    • o ubiquinol oxidase from Escherichia coli. An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center. Biochemistry. 32:1993;11173-11180.
    • (1993) Biochemistry , vol.32 , pp. 11173-11180
    • Thomas, J.W.1    Lemieux, L.J.2    Alben, J.O.3    Gennis, R.B.4
  • 45
    • 0028913025 scopus 로고
    • 3 ubiquinol oxidase of Escherichia coli: Second-site mutations in subunit I that restore proton pumping in the mutant Asp 135→Asn
    • 3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp 135→Asn. Biochemistry. 34:1995;4428-4433.
    • (1995) Biochemistry , vol.34 , pp. 4428-4433
    • Garcia-Horsman, J.A.1    Puustinen, A.2    Gennis, R.B.3    Wikström, M.4
  • 46
    • 0027491552 scopus 로고
    • Substitution of asparagine-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, Wikström M. Substitution of asparagine-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
    • 0028941458 scopus 로고
    • Possible proton relay pathways in cytochrome c oxidase
    • of special interest. Mutation of Asp132 in subunit I of the COX from Rhodobacter sphaeroides leads to the loss of proton-pumping activity but the retention of electron-transfer activity. Evidence for separated pathways for consumed and pumped protons is presented.
    • of special interest Fetter JR, Qian J, Shapleigh J, Thomas JW, Garcia-Horsman A, Schmidt E, Hosler J, Babcock GT, Gennis RB. Possible proton relay pathways in cytochrome c oxidase. Proc Natl Acad Sci USA. 92:1995;1604-1608 Mutation of Asp132 in subunit I of the COX from Rhodobacter sphaeroides leads to the loss of proton-pumping activity but the retention of electron-transfer activity. Evidence for separated pathways for consumed and pumped protons is presented.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1604-1608
    • Fetter, J.R.1    Qian, J.2    Shapleigh, J.3    Thomas, J.W.4    Garcia-Horsman, A.5    Schmidt, E.6    Hosler, J.7    Babcock, G.T.8    Gennis, R.B.9
  • 48
    • 0028851789 scopus 로고
    • The interaction of cytochrome oxidase with hydrogen peroxide: The relationship of compounds P and F
    • Fabian M, Palmer G. The interaction of cytochrome oxidase with hydrogen peroxide: the relationship of compounds P and F. Biochemistry. 34:1995;13802-13810.
    • (1995) Biochemistry , vol.34 , pp. 13802-13810
    • Fabian, M.1    Palmer, G.2
  • 49
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidised cytochrome c oxidase at 2.8 Å
    • of outstanding interest. The structure of the 13 protein subunits of COX from bovine heart mitochondria, their interactions and the binding of lipids are described. Pathways for proton transfer and oxygen diffusion are suggested.
    • of outstanding interest Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaona R, Yoshikawa S. The whole structure of the 13-subunit oxidised cytochrome c oxidase at 2.8 Å Science. 272:1996;1136-1144 The structure of the 13 protein subunits of COX from bovine heart mitochondria, their interactions and the binding of lipids are described. Pathways for proton transfer and oxygen diffusion are suggested.
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1    Aoyama, H.2    Yamashita, E.3    Tomizaki, T.4    Yamaguchi, H.5    Shinzawa-Itoh, K.6    Nakashima, R.7    Yaona, R.8    Yoshikawa, S.9


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