메뉴 건너뛰기




Volumn 44, Issue 37, 2005, Pages 12391-12401

Cytochrome c oxidase as a calcium binding protein. Studies on the role of a conserved aspartate in helices XI-XII cytoplasmic loop in cation binding

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CALCIUM; CYTOLOGY; MOLECULAR STRUCTURE;

EID: 24944511130     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050376v     Document Type: Article
Times cited : (24)

References (43)
  • 1
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock, G. T., and Wikstrom, M. (1992) Oxygen activation and the conservation of energy in cell respiration, Nature 356, 301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikstrom, M.2
  • 2
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson-Miller, S., and Babcock, G. T. (1996) Heme/copper terminal oxidases, Chem. Rev. 7, 2889-2907.
    • (1996) Chem. Rev. , vol.7 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 5
    • 0642283837 scopus 로고    scopus 로고
    • Cytochrome c oxidase - Structure, function, and physiology of a redox driven molecular machine
    • Richter, O.-M. H., and Ludwig, B. (2003) Cytochrome c oxidase - structure, function, and physiology of a redox driven molecular machine, Rev. Physiol. Biochem. Pharmacol. 147, 47-74.
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.147 , pp. 47-74
    • Richter, O.-M.H.1    Ludwig, B.2
  • 9
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B., and Michel, H. (1995) Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans, Nature 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 10
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody fv fragment
    • Ostermeier, C., Harrenga, A., Ermler, U., and Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody fv fragment, Proc. Natl. Acad. Sci. U.S.A. 94, 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
  • 12
    • 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., and Iwata, S. (2002) The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides, J. Mol. Biol. 321, 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
  • 13
    • 0001397720 scopus 로고    scopus 로고
    • The role of magnesium and its associated water channel in activity and regulation of cytochrome c oxidase
    • (Peschek, G. E. A., Ed.), Kluwer Academic/Plenum Publishers, New York
    • Florens, L., Hoganson, C., McCracken, J., Fetter, J., Mills, D., Babcock, G. T., and Ferguson-Miller, S. (1999) The role of magnesium and its associated water channel in activity and regulation of cytochrome c oxidase, in The Photosynthetic Procaryotes (Peschek, G. E. A., Ed.) pp 329-339, Kluwer Academic/Plenum Publishers, New York.
    • (1999) The Photosynthetic Procaryotes , pp. 329-339
    • Florens, L.1    Hoganson, C.2    McCracken, J.3    Fetter, J.4    Mills, D.5    Babcock, G.T.6    Ferguson-Miller, S.7
  • 14
    • 0035954401 scopus 로고    scopus 로고
    • Fast deuterium access to the buried magnesium/manganese site in cytochrome c oxidase
    • Florens, L., Schmidt, B., McCracken, J., and Ferguson-Miller, S. (2001 ) Fast deuterium access to the buried magnesium/manganese site in cytochrome c oxidase, Biochemistry 40, 7491-7497.
    • (2001) Biochemistry , vol.40 , pp. 7491-7497
    • Florens, L.1    Schmidt, B.2    McCracken, J.3    Ferguson-Miller, S.4
  • 15
    • 0346103674 scopus 로고    scopus 로고
    • A discrete water exit pathway in the membrane protein cytochrome c oxidase
    • Schmidt, B., McCracken, J., and Ferguson-Miller, S. (2003) A discrete water exit pathway in the membrane protein cytochrome c oxidase, Proc. Natl. Acad. Sci. U.S.A. 100, 15539-15542.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 15539-15542
    • Schmidt, B.1    McCracken, J.2    Ferguson-Miller, S.3
  • 16
    • 0016759109 scopus 로고
    • A spectral shift of heme a induced by calcium ions
    • Wikstrom, M., and Saari, H. (1975) A spectral shift of heme a induced by calcium ions, Biochim. Biophys. Acta 408, 170-179.
    • (1975) Biochim. Biophys. Acta , vol.408 , pp. 170-179
    • Wikstrom, M.1    Saari, H.2
  • 18
    • 0025117370 scopus 로고
    • 2+-dependent red shift of cytochrome a. Is there a hydronium output well in cytochrome c oxidase?
    • 2+-dependent red shift of cytochrome a. Is there a hydronium output well in cytochrome c oxidase?, Biochem. Int. 20, 183-190.
    • (1990) Biochem. Int. , vol.20 , pp. 183-190
    • Mkrtchyan, H.1    Vygodina, T.2    Konstantinov, A.A.3
  • 22
    • 0033578348 scopus 로고    scopus 로고
    • The calcium binding site in cytochrome aas from Paracoccus denitrificans
    • Riistama, S., Laakkonen, L., Wikstrom, M., Verkhovsky, M. I., and Puustinen, A. (1999) The calcium binding site in cytochrome aas from Paracoccus denitrificans, Biochemistry 38, 10670-10677.
    • (1999) Biochemistry , vol.38 , pp. 10670-10677
    • Riistama, S.1    Laakkonen, L.2    Wikstrom, M.3    Verkhovsky, M.I.4    Puustinen, A.5
  • 23
  • 25
    • 0001693643 scopus 로고
    • A rapid method for the preparation of highly purified cytochrome oxidase
    • Fowler, L. R., Richardson, S. H., and Hatefi, Y. (1962) A rapid method for the preparation of highly purified cytochrome oxidase, Biochim. Biophys. Acta 64, 170-173.
    • (1962) Biochim. Biophys. Acta , vol.64 , pp. 170-173
    • Fowler, L.R.1    Richardson, S.H.2    Hatefi, Y.3
  • 26
    • 0010577232 scopus 로고
    • The isolation of a copper protein from cytochrome oxidase
    • MacLennan, D. H.: and Tzagoloff, A. (1965) The isolation of a copper protein from cytochrome oxidase, Biochim. Biophys. Acta 96, 166-168.
    • (1965) Biochim. Biophys. Acta , vol.96 , pp. 166-168
    • MacLennan, D.H.1    Tzagoloff, A.2
  • 27
    • 0033741298 scopus 로고    scopus 로고
    • X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase
    • Yoshikawa, S., Shinzawa-Itoh, K., and Tsukihara, T. (2000) X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase, J. Inorg. Biochem. 82, 1-7.
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 1-7
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Tsukihara, T.3
  • 29
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • Pereira, M. M., Santana, M., and Teixeira, M. (2001) A novel scenario for the evolution of haem-copper oxygen reductases, Biochim. Biophys. Acta 1505, 185-208.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 31
    • 0035702819 scopus 로고    scopus 로고
    • New control of mitochondrial membrane potential and ROS formation
    • Lee, I., Bender, E., Arnold, S., and Kadenbach, B. (2001) New control of mitochondrial membrane potential and ROS formation, Biol. Chem. 382, 1629-1636.
    • (2001) Biol. Chem. , vol.382 , pp. 1629-1636
    • Lee, I.1    Bender, E.2    Arnold, S.3    Kadenbach, B.4
  • 32
    • 3543041902 scopus 로고    scopus 로고
    • Thermodynamic and choreographic constraints for energy transduction by cytochrome c oxidase
    • Xavier, A. V. (2004) Thermodynamic and choreographic constraints for energy transduction by cytochrome c oxidase, Biochim. Biophys. Acta 1658, 23-30.
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 23-30
    • Xavier, A.V.1
  • 34
    • 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 reveals modulation of the properties of heme a
    • Lee, H.-M., Das, T. K., Rousseau, D. L., Mills, D., Fergusson-Miller, S., and Gennis, R. (2000) 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 reveals modulation of the properties of heme a. Biochemistry 39, 2989-2996.
    • (2000) Biochemistry , vol.39 , pp. 2989-2996
    • Lee, H.-M.1    Das, T.K.2    Rousseau, D.L.3    Mills, D.4    Fergusson-Miller, S.5    Gennis, R.6
  • 35
    • 18744417510 scopus 로고
    • Role of protons in the mechanism of coupling site 111 of the mitochondrial respiratory chain: Cytochrome oxidase as an electronic-protonic generator of membrane potential
    • Konstantinov, A. A. (1977) Role of protons in the mechanism of coupling site 111 of the mitochondrial respiratory chain: cytochrome oxidase as an electronic-protonic generator of membrane potential, Dokl. Akad. Nauk SSSR 237, 713-716.
    • (1977) Dokl. Akad. Nauk SSSR , vol.237 , pp. 713-716
    • Konstantinov, A.A.1
  • 36
    • 0017883558 scopus 로고
    • Involvement of intramitochondrial protons in redox rections of cytochrome a
    • Artzatbanov, V. Y., Konstantinov, A. A., and Skulachev, V. P. (1978) Involvement of intramitochondrial protons in redox rections of cytochrome a, FEBS Lett. 87, 180-185.
    • (1978) FEBS Lett. , vol.87 , pp. 180-185
    • Artzatbanov, V.Y.1    Konstantinov, A.A.2    Skulachev, V.P.3
  • 37
    • 0032573072 scopus 로고    scopus 로고
    • The mechanism of proton pumping by cytochrome c oxidase
    • Michel, H. (1998) The mechanism of proton pumping by cytochrome c oxidase, Proc. Natl. Acad. Sci. U.S.A. 95, 12819-12824.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12819-12824
    • Michel, H.1
  • 39
    • 1942472174 scopus 로고    scopus 로고
    • A cooperative model for proton pumping in cytochrome c oxidase
    • Papa, S., Capitanio, N., and Capitanio, G. (2004) A cooperative model for proton pumping in cytochrome c oxidase., Biochim. Biophys. Acta 1655, 353-364.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 353-364
    • Papa, S.1    Capitanio, N.2    Capitanio, G.3
  • 40
    • 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. (2002) A mechano-chemical model for energy transduction in cytochrome c oxidase: the work of a Maxwell's God, FEBS Lett. 532, 261-266.
    • (2002) FEBS Lett. , vol.532 , pp. 261-266
    • Xavier, A.V.1
  • 41
    • 0032564864 scopus 로고    scopus 로고
    • Uncoupling: New approaches to an old problem of bioenergetics
    • Skulachev, V. P. (1998) Uncoupling: new approaches to an old problem of bioenergetics, Biochim. Biophys. Acta 1363, 100-124.
    • (1998) Biochim. Biophys. Acta , vol.1363 , pp. 100-124
    • Skulachev, V.P.1
  • 42
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson, R. B., and Kemp, B. E. (1991) Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations, Methods Enzymol. 200, 62-81.
    • (1991) Methods Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.