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Volumn 1817, Issue 4, 2012, Pages 666-671

The rate-limiting step in O 2 reduction by cytochrome ba 3 from Thermus thermophilus

Author keywords

Bioenergetics; Cytochrome oxidase; Raman scattering; Stopped flow

Indexed keywords

CYTOCHROME; CYTOCHROME BA3; HEME A3; HEME DERIVATIVE; OXIDOREDUCTASE; OXYGEN; UNCLASSIFIED DRUG;

EID: 84857914894     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.11.010     Document Type: Article
Times cited : (6)

References (32)
  • 1
    • 0037031484 scopus 로고    scopus 로고
    • Observation of the equilibrium CuB-CO complex and functional implications of the transient heme a3 propionates in cytochrome ba3-CO from Thermus thermophilus. Fourier transform infrared (FTIR) and time-resolved step-scan FTIR studies
    • K. Koutsoupakis, S. Stavrakis, E. Pinakoulaki, T. Soulimane, and C. Varotsis Observation of the equilibrium CuB-CO complex and functional implications of the transient heme a3 propionates in cytochrome ba3-CO from Thermus thermophilus. Fourier transform infrared (FTIR) and time-resolved step-scan FTIR studies J. Biol. Chem. 277 2002 32860 32866
    • (2002) J. Biol. Chem. , vol.277 , pp. 32860-32866
    • Koutsoupakis, K.1    Stavrakis, S.2    Pinakoulaki, E.3    Soulimane, T.4    Varotsis, C.5
  • 4
    • 2542460189 scopus 로고    scopus 로고
    • Simultaneous resonance Raman detection of the heme a3-Fe-CO and CuB-CO species in CO-bound ba3-cytochrome c oxidase from Thermus thermophilus. Evidence for a charge transfer CuB-CO transition
    • E. Pinakoulaki, T. Ohta, T. Soulimane, T. Kitagawa, and C. Varotsis Simultaneous resonance Raman detection of the heme a3-Fe-CO and CuB-CO species in CO-bound ba3-cytochrome c oxidase from Thermus thermophilus. Evidence for a charge transfer CuB-CO transition J. Biol. Chem. 279 2004 22791 22794
    • (2004) J. Biol. Chem. , vol.279 , pp. 22791-22794
    • Pinakoulaki, E.1    Ohta, T.2    Soulimane, T.3    Kitagawa, T.4    Varotsis, C.5
  • 6
    • 14844336371 scopus 로고    scopus 로고
    • A homologous expression system for obtaining engineered cytochrome ba3 from Thermus thermophilus HB8
    • Y. Chen, L. Hunsicker-Wang, R.L. Pacoma, E. Luna, and J.A. Fee A homologous expression system for obtaining engineered cytochrome ba3 from Thermus thermophilus HB8 Protein Expr. Purif. 40 2005 299 318
    • (2005) Protein Expr. Purif. , vol.40 , pp. 299-318
    • Chen, Y.1    Hunsicker-Wang, L.2    Pacoma, R.L.3    Luna, E.4    Fee, J.A.5
  • 7
    • 0017727697 scopus 로고
    • An infrared study of CO binding to heart cytochrome c oxidase and hemoglobin A. Implications re O2 reactions
    • S. Yoshikawa, M.G. Choc, M.C. O'Toole, and W.S. Caughey An infrared study of CO binding to heart cytochrome c oxidase and hemoglobin A. Implications re O2 reactions J. Biol. Chem. 252 1977 5498 5508
    • (1977) J. Biol. Chem. , vol.252 , pp. 5498-5508
    • Yoshikawa, S.1    Choc, M.G.2    O'Toole, M.C.3    Caughey, W.S.4
  • 8
    • 0020490631 scopus 로고
    • Cytochrome c oxidase binding of hydrogen peroxide
    • D. Bickar, J. Bonaventura, and C. Bonaventura Cytochrome c oxidase binding of hydrogen peroxide Biochemistry 21 1982 2661 2666
    • (1982) Biochemistry , vol.21 , pp. 2661-2666
    • Bickar, D.1    Bonaventura, J.2    Bonaventura, C.3
  • 9
    • 27744531901 scopus 로고    scopus 로고
    • Structural characterization of the [Pco/o(2)] compound of cytochrome c oxidase
    • H. Ji, S.R. Yeh, and D.L. Rousseau Structural characterization of the [Pco/o(2)] compound of cytochrome c oxidase FEBS Lett. 579 2005 6361 6364
    • (2005) FEBS Lett. , vol.579 , pp. 6361-6364
    • Ji, H.1    Yeh, S.R.2    Rousseau, D.L.3
  • 10
    • 0017845014 scopus 로고
    • Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichlorophenolindophenol and potassium ferricyanide by L-ascorbic acid
    • B. Tonomura, H. Nakatani, M. Ohnishi, J. Yamaguchi-Ito, and K. Hiromi Test reactions for a stopped-flow apparatus. Reduction of 2,6- dichlorophenolindophenol and potassium ferricyanide by L-ascorbic acid Anal. Biochem. 84 1978 370 383
    • (1978) Anal. Biochem. , vol.84 , pp. 370-383
    • Tonomura, B.1    Nakatani, H.2    Ohnishi, M.3    Yamaguchi-Ito, J.4    Hiromi, K.5
  • 12
    • 0026787165 scopus 로고
    • Magnetic circular dichroism study of cytochrome ba3 from Thermus thermophilus: Spectral contributions from cytochromes b and a3 and nanosecond spectroscopy of CO photodissociation intermediates
    • R.A. Goldbeck, O. Einarsdottir, T.D. Dawes, D.B. O'Connor, K.K. Surerus, J.A. Fee, and D.S. Kliger Magnetic circular dichroism study of cytochrome ba3 from Thermus thermophilus: spectral contributions from cytochromes b and a3 and nanosecond spectroscopy of CO photodissociation intermediates Biochemistry 31 1992 9376 9387
    • (1992) Biochemistry , vol.31 , pp. 9376-9387
    • Goldbeck, R.A.1    Einarsdottir, O.2    Dawes, T.D.3    O'Connor, D.B.4    Surerus, K.K.5    Fee, J.A.6    Kliger, D.S.7
  • 13
    • 33646951046 scopus 로고    scopus 로고
    • Electron transfer among the CuA-, heme b- and a3-centers of Thermus thermophilus cytochrome ba3
    • O. Farver, Y. Chen, J.A. Fee, and I. Pecht Electron transfer among the CuA-, heme b- and a3-centers of Thermus thermophilus cytochrome ba3 FEBS Lett. 580 2006 3417 3421
    • (2006) FEBS Lett. , vol.580 , pp. 3417-3421
    • Farver, O.1    Chen, Y.2    Fee, J.A.3    Pecht, I.4
  • 15
    • 0343539036 scopus 로고    scopus 로고
    • The active site structure of ba3 oxidase from Thermus thermophilus studied by resonance raman spectroscopy
    • S. Gerscher, P. Hildebrandt, G. Buse, and T. Soulimane The active site structure of ba3 oxidase from Thermus thermophilus studied by resonance raman spectroscopy Biospectroscopy 5 1999 S53 S63
    • (1999) Biospectroscopy , vol.5
    • Gerscher, S.1    Hildebrandt, P.2    Buse, G.3    Soulimane, T.4
  • 16
    • 0028293629 scopus 로고
    • Spectroscopic characterization of cytochrome ba3, a terminal oxidase from Thermus thermophilus: Comparison of the a3/CuB site to that of bovine cytochrome aa3
    • W.A. Oertling, K.K. Surerus, O. Einarsdottir, J.A. Fee, R.B. Dyer, and W.H. Woodruff Spectroscopic characterization of cytochrome ba3, a terminal oxidase from Thermus thermophilus: comparison of the a3/CuB site to that of bovine cytochrome aa3 Biochemistry 33 1994 3128 3141
    • (1994) Biochemistry , vol.33 , pp. 3128-3141
    • Oertling, W.A.1    Surerus, K.K.2    Einarsdottir, O.3    Fee, J.A.4    Dyer, R.B.5    Woodruff, W.H.6
  • 17
    • 0024385889 scopus 로고
    • Resonance Raman spectra of bovine liver catalase compound II. Similarity of the heme environment to horseradish peroxidase compound II
    • W.J. Chuang, J. Heldt, and H.E. Van Wart Resonance Raman spectra of bovine liver catalase compound II. Similarity of the heme environment to horseradish peroxidase compound II J. Biol. Chem. 264 1989 14209 14215
    • (1989) J. Biol. Chem. , vol.264 , pp. 14209-14215
    • Chuang, W.J.1    Heldt, J.2    Van Wart, H.E.3
  • 18
    • 0002153672 scopus 로고
    • Infrared and Raman spectra of metalloporphyrins
    • T. Kitagawa, and Y. Ozaki Infrared and Raman spectra of metalloporphyrins Struct. Bonding 64 1987 71 114
    • (1987) Struct. Bonding , vol.64 , pp. 71-114
    • Kitagawa, T.1    Ozaki, Y.2
  • 19
    • 0021777960 scopus 로고
    • Resonance Raman spectroscopy as a probe of heme protein structure and dynamics
    • T.G. Spiro Resonance Raman spectroscopy as a probe of heme protein structure and dynamics Adv. Protein Chem. 37 1985 111 159
    • (1985) Adv. Protein Chem. , vol.37 , pp. 111-159
    • Spiro, T.G.1
  • 20
    • 33749137961 scopus 로고    scopus 로고
    • Transmembrane proton translocation by cytochrome c oxidase
    • G. Branden, R.B. Gennis, and P. Brzezinski Transmembrane proton translocation by cytochrome c oxidase Biochim. Biophys. Acta 1757 2006 1052 1063
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1052-1063
    • Branden, G.1    Gennis, R.B.2    Brzezinski, P.3
  • 21
    • 0007576881 scopus 로고    scopus 로고
    • Time-resolved resonance Raman study of dioxygen reduction by cytochrome c oxidase
    • T. Kitagawa, and T. Ogura Time-resolved resonance Raman study of dioxygen reduction by cytochrome c oxidase Pure Appl. Chem. 70 1998 881 888
    • (1998) Pure Appl. Chem. , vol.70 , pp. 881-888
    • Kitagawa, T.1    Ogura, T.2
  • 22
    • 0003097351 scopus 로고
    • Raman difference spectroscopy as a probe of biological molecules
    • D.L. Rousseau Raman difference spectroscopy as a probe of biological molecules J. Raman. Spectrosc. 10 1981 94 99
    • (1981) J. Raman. Spectrosc. , vol.10 , pp. 94-99
    • Rousseau, D.L.1
  • 23
    • 0141814916 scopus 로고    scopus 로고
    • Docking site dynamics of ba3-cytochrome c oxidase from Thermus thermophilus
    • C. Koutsoupakis, T. Soulimane, and C. Varotsis Docking site dynamics of ba3-cytochrome c oxidase from Thermus thermophilus J. Biol. Chem. 278 2003 36806 36809
    • (2003) J. Biol. Chem. , vol.278 , pp. 36806-36809
    • Koutsoupakis, C.1    Soulimane, T.2    Varotsis, C.3
  • 24
    • 42349083650 scopus 로고    scopus 로고
    • Crystallographic studies of Xe and Kr binding within the large internal cavity of cytochrome ba3 from Thermus thermophilus: Structural analysis and role of oxygen transport channels in the heme-Cu oxidases
    • V.M. Luna, Y. Chen, J.A. Fee, and C.D. Stout Crystallographic studies of Xe and Kr binding within the large internal cavity of cytochrome ba3 from Thermus thermophilus: structural analysis and role of oxygen transport channels in the heme-Cu oxidases Biochemistry 47 2008 4657 4665
    • (2008) Biochemistry , vol.47 , pp. 4657-4665
    • Luna, V.M.1    Chen, Y.2    Fee, J.A.3    Stout, C.D.4
  • 25
    • 61449123035 scopus 로고    scopus 로고
    • Combined microspectrophotometric and crystallographic examination of chemically reduced and X-ray radiation-reduced forms of cytochrome ba3 oxidase from Thermus thermophilus: Structure of the reduced form of the enzyme
    • B. Liu, Y. Chen, T. Doukov, S.M. Soltis, C.D. Stout, and J.A. Fee Combined microspectrophotometric and crystallographic examination of chemically reduced and X-ray radiation-reduced forms of cytochrome ba3 oxidase from Thermus thermophilus: structure of the reduced form of the enzyme Biochemistry 48 2009 820 826
    • (2009) Biochemistry , vol.48 , pp. 820-826
    • Liu, B.1    Chen, Y.2    Doukov, T.3    Soltis, S.M.4    Stout, C.D.5    Fee, J.A.6
  • 26
    • 0027308712 scopus 로고
    • Coordination dynamics of heme-copper oxidases. the ligand shuttle and the control and coupling of electron transfer and proton translocation
    • W.H. Woodruff Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation J. Bioenerg. Biomembr. 25 1993 177 188
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 177-188
    • Woodruff, W.H.1
  • 27
    • 0026778190 scopus 로고
    • Reaction of dioxygen with cytochrome c oxidase reduced to different degrees: Indications of a transient dioxygen complex with copper-B
    • M. Oliveberg, and B.G. Malmstrom Reaction of dioxygen with cytochrome c oxidase reduced to different degrees: indications of a transient dioxygen complex with copper-B Biochemistry 31 1992 3560 3563
    • (1992) Biochemistry , vol.31 , pp. 3560-3563
    • Oliveberg, M.1    Malmstrom, B.G.2
  • 28
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • M.I. Verkhovsky, J.E. Morgan, and M. Wikstrom Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase Biochemistry 33 1994 3079 3086
    • (1994) Biochemistry , vol.33 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikstrom, M.3
  • 29
    • 0026038522 scopus 로고
    • Studies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase
    • R.S. Blackmore, C. Greenwood, and Q.H. Gibson Studies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase J. Biol. Chem. 266 1991 19245 19249
    • (1991) J. Biol. Chem. , vol.266 , pp. 19245-19249
    • Blackmore, R.S.1    Greenwood, C.2    Gibson, Q.H.3
  • 30
    • 0035042514 scopus 로고    scopus 로고
    • PH-dependent structural changes at the heme-copper binuclear center of cytochrome c oxidase
    • T.K. Das, F.L. Tomson, R.B. Gennis, M. Gordon, and D.L. Rousseau pH-dependent structural changes at the heme-copper binuclear center of cytochrome c oxidase Biophys. J. 80 2001 2039 2045
    • (2001) Biophys. J. , vol.80 , pp. 2039-2045
    • Das, T.K.1    Tomson, F.L.2    Gennis, R.B.3    Gordon, M.4    Rousseau, D.L.5
  • 31
    • 73149105493 scopus 로고    scopus 로고
    • Communication between R481 and Cu(B) in cytochrome bo(3) ubiquinol oxidase from Escherichia coli
    • T. Egawa, M.T. Lin, J.P. Hosler, R.B. Gennis, S.R. Yeh, and D.L. Rousseau Communication between R481 and Cu(B) in cytochrome bo(3) ubiquinol oxidase from Escherichia coli Biochemistry 48 2009 12113 12124
    • (2009) Biochemistry , vol.48 , pp. 12113-12124
    • Egawa, T.1    Lin, M.T.2    Hosler, J.P.3    Gennis, R.B.4    Yeh, S.R.5    Rousseau, D.L.6
  • 32
    • 77149166317 scopus 로고    scopus 로고
    • Modulation of the active site conformation by site-directed mutagenesis in cytochrome c oxidase from Paracoccus denitrificans
    • H. Ji, T.K. Das, A. Puustinen, M. Wikstrom, S.R. Yeh, and D.L. Rousseau Modulation of the active site conformation by site-directed mutagenesis in cytochrome c oxidase from Paracoccus denitrificans J. Inorg. Biochem. 104 2010 318 323
    • (2010) J. Inorg. Biochem. , vol.104 , pp. 318-323
    • Ji, H.1    Das, T.K.2    Puustinen, A.3    Wikstrom, M.4    Yeh, S.R.5    Rousseau, D.L.6


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