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Volumn 579, Issue 14, 2005, Pages 3014-3018

Photothermal studies of CO photodissociation from mixed valence Escherichia coli cytochrome bo3

Author keywords

Cytochrome bo3 oxidase; Electron transfer; Mixed valence; Photoacustic calorimetry

Indexed keywords

BACTERIAL ENZYME; CARBON MONOXIDE; COPPER; CYTOCHROME B OXIDASE; HEME; UNCLASSIFIED DRUG;

EID: 20444373304     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.04.055     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0033734197 scopus 로고    scopus 로고
    • Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers
    • M. Tsubaki, H. Hori, and T. Mogi Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers J. Inorg. Biochem. 82 2000 19 25
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 19-25
    • Tsubaki, M.1    Hori, H.2    Mogi, T.3
  • 2
    • 0026438826 scopus 로고
    • The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type
    • A. Puustinen, J.E. Morgan, M. Verkhovski, J.W. Thomas, and R.B. Gennis The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type Biochemistry 31 1992 10363 10369
    • (1992) Biochemistry , vol.31 , pp. 10363-10369
    • Puustinen, A.1    Morgan, J.E.2    Verkhovski, M.3    Thomas, J.W.4    Gennis, R.B.5
  • 3
    • 0001383847 scopus 로고
    • The aerobic respiratory chain of Escherichia coli
    • Y. Anraku, and R.B. Gennis The aerobic respiratory chain of Escherichia coli TIBS 12 1987 262 266
    • (1987) TIBS , vol.12 , pp. 262-266
    • Anraku, Y.1    Gennis, R.B.2
  • 6
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: Progress, problems and postulates
    • D. Zaslavski, and R.B. Gennis Proton pumping by cytochrome oxidase: progress, problems and postulates Biochim. Biophys. Acta 1458 2000 164 179
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavski, D.1    Gennis, R.B.2
  • 7
    • 0022974929 scopus 로고
    • The proton-pumping site of cytochrome c oxidase: A model of its structure and mechanism
    • J. Gelles, D.F. Blair, and S.I. Chan The proton-pumping site of cytochrome c oxidase: a model of its structure and mechanism Biochim. Biophys. Acta 853 1986 205 236
    • (1986) Biochim. Biophys. Acta , vol.853 , pp. 205-236
    • Gelles, J.1    Blair, D.F.2    Chan, S.I.3
  • 9
    • 0027383797 scopus 로고
    • Intramolecular electron transfer in cytochrome o of Escherichia coli: Events following the photolysis of fully and partially reduced CO-bound forms of the bo3 and oo3 enzymes
    • J.E. Morgan, M.I. Verkhovsky, A. Puustinen, and M. Wikstrom Intramolecular electron transfer in cytochrome o of Escherichia coli: events following the photolysis of fully and partially reduced CO-bound forms of the bo3 and oo3 enzymes Biochemistry 32 1993 11413 11418
    • (1993) Biochemistry , vol.32 , pp. 11413-11418
    • Morgan, J.E.1    Verkhovsky, M.I.2    Puustinen, A.3    Wikstrom, M.4
  • 10
    • 0028089286 scopus 로고
    • Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli
    • S. Brown, J.N. Rumbley, J.A. Moody, J.W. Thomas, R.B. Gennis, and P.R. Rich Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli Biochim. Biophys. Acta 1183 1994 521 532
    • (1994) Biochim. Biophys. Acta , vol.1183 , pp. 521-532
    • Brown, S.1    Rumbley, J.N.2    Moody, J.A.3    Thomas, J.W.4    Gennis, R.B.5    Rich, P.R.6
  • 12
    • 0024448807 scopus 로고
    • Electron transfer between cytochrome a and copper a in cytochrome c oxidase: A perturbed equilibrium study
    • J.E. Morgan, P.M. Li, D. Jang, M.A. El-Sayed, and S.I. Chan Electron transfer between cytochrome a and copper A in cytochrome c oxidase: a perturbed equilibrium study Biochemistry 28 1989 6975 6983
    • (1989) Biochemistry , vol.28 , pp. 6975-6983
    • Morgan, J.E.1    Li, P.M.2    Jang, D.3    El-Sayed, M.A.4    Chan, S.I.5
  • 13
    • 0028925948 scopus 로고
    • Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides
    • P. Adelroth, P. Brzezinski, and B.G. Malmstron Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides Biochemistry 34 1995 2844 2849
    • (1995) Biochemistry , vol.34 , pp. 2844-2849
    • Adelroth, P.1    Brzezinski, P.2    Malmstron, B.G.3
  • 16
    • 0023196745 scopus 로고
    • Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli
    • D.C.-T. Au, and R.B. Gennis Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli J. Bacteriol. 169 1987 3237 3242
    • (1987) J. Bacteriol. , vol.169 , pp. 3237-3242
    • Au, D.C.-T.1    Gennis, R.B.2
  • 17
    • 0342378077 scopus 로고    scopus 로고
    • One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase
    • J.N. Rumbley, E.F. Nickels, and R.B. Gennis One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase Biochim. Biophys. Acta 1340 1997 131 142
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 131-142
    • Rumbley, J.N.1    Nickels, E.F.2    Gennis, R.B.3
  • 18
    • 2342526764 scopus 로고
    • Time-resolved photothermal and photoacoustic methods applied to photoinduced processes in solution
    • S.E. Braslavky, and G.E. Heibel Time-resolved photothermal and photoacoustic methods applied to photoinduced processes in solution Chem. Rev. 92 1992 1381 1410
    • (1992) Chem. Rev. , vol.92 , pp. 1381-1410
    • Braslavky, S.E.1    Heibel, G.E.2
  • 19
    • 0035760615 scopus 로고    scopus 로고
    • Photothermal methods applied to energy transducing membrane proteins: A review
    • B.D. Barker, and R.W. Larsen Photothermal methods applied to energy transducing membrane proteins: a review J. Biochem. Mol. Biol. Biophys. 5 2001 407 434
    • (2001) J. Biochem. Mol. Biol. Biophys. , vol.5 , pp. 407-434
    • Barker, B.D.1    Larsen, R.W.2
  • 20
    • 0037277526 scopus 로고    scopus 로고
    • Structure-function relationships in metalloproteins
    • Marriott, G. and Parker, I., Eds.
    • Miksovska, J. and Larsen, R.W. (2003) Structure-function relationships in metalloproteins. In: Methods in Enzymology: Biophotonics (Marriott, G. and Parker, I., Eds.), Vol. 360, part A, pp. 302-329
    • (2003) Methods in Enzymology: Biophotonics , vol.360 , Issue.PART A , pp. 302-329
    • Miksovska, J.1    Larsen, R.W.2
  • 21
    • 0025729408 scopus 로고
    • Time-resolved photoacoustic calorimetry: A study of myoglobin and rhodopsin
    • K.S. Peters, T. Watson, and K. Mar Time-resolved photoacoustic calorimetry: a study of myoglobin and rhodopsin Annu. Rev. Biophys. Chem. 20 1991 343 362
    • (1991) Annu. Rev. Biophys. Chem. , vol.20 , pp. 343-362
    • Peters, K.S.1    Watson, T.2    Mar, K.3
  • 22
  • 23
    • 0033137318 scopus 로고    scopus 로고
    • Coordination of CuB in reduced and CO-liganded states of cytochrome bo3 from Escherichia coli. Is chloride ion a cofactor?
    • M. Ralle, M.l. Verkhovskaya, J.E. Morgan, M.I. Verkhovsky, M. Winkstrom, and N.J. Blackburn Coordination of CuB in reduced and CO-liganded states of cytochrome bo3 from Escherichia coli. Is chloride ion a cofactor? Biochemistry 38 1999 7185 7194
    • (1999) Biochemistry , vol.38 , pp. 7185-7194
    • Ralle, M.1    Verkhovskaya, M.L.2    Morgan, J.E.3    Verkhovsky, M.I.4    Winkstrom, M.5    Blackburn, N.J.6
  • 24
    • 33845556564 scopus 로고
    • Synthetic model compounds for hemoproteins
    • T.G. Traylor Synthetic model compounds for hemoproteins Acc. Chem. Res. 14 1981 109 116
    • (1981) Acc. Chem. Res. , vol.14 , pp. 109-116
    • Traylor, T.G.1
  • 25
    • 0035519279 scopus 로고    scopus 로고
    • Ultrafast haem-haem electron transfer in cytochrome c oxidase
    • M.I. Verkhovsky, A. Jasaitis, and M. Wikstrom Ultrafast haem-haem electron transfer in cytochrome c oxidase Biochim. Biophys. Acta 1506 2001 143 146
    • (2001) Biochim. Biophys. Acta , vol.1506 , pp. 143-146
    • Verkhovsky, M.I.1    Jasaitis, A.2    Wikstrom, M.3
  • 26
    • 9244257845 scopus 로고    scopus 로고
    • Electron transfer between hemes in mammalian cytochrome c oxidase
    • E. Pilet, A. Jasaitis, U. Liebl, and M.H. Vos Electron transfer between hemes in mammalian cytochrome c oxidase Proc. Natl. Acad. Sci. USA 101/46 2004 16198 16203
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.46 , pp. 16198-16203
    • Pilet, E.1    Jasaitis, A.2    Liebl, U.3    Vos, M.H.4
  • 27
    • 0037143546 scopus 로고    scopus 로고
    • The rate of internal heme-heme electron transfer in cytochrome C oxidase
    • A. Namslauer, M. Branden, and P. Brzezinski The rate of internal heme-heme electron transfer in cytochrome C oxidase Biochemistry 41 2002 10369 10374
    • (2002) Biochemistry , vol.41 , pp. 10369-10374
    • Namslauer, A.1    Branden, M.2    Brzezinski, P.3
  • 29
    • 0036219767 scopus 로고    scopus 로고
    • B in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: A time-resolved step-scan Fourier transform infrared investigation
    • B in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: a time-resolved step-scan Fourier transform infrared investigation Biophys. J. 82 2002 1 10
    • (2002) Biophys. J. , vol.82 , pp. 1-10
    • Heitbrink, D.1    Sigurdson, H.2    Bolwien, C.3    Brzeninski, P.4    Heberle, J.5
  • 30
    • 0037176910 scopus 로고    scopus 로고
    • Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo(3) from Escherichia coli
    • J.A. Bailey, F.L. Tomson, S.L. Mecklenburg, G.M. MacDonald, A. Katsonouri, A. Puustinen, R.B. Gennis, W.H. Woodruff, and R.B. Dyer Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo(3) from Escherichia coli Biochemistry 41 2002 2675 2683
    • (2002) Biochemistry , vol.41 , pp. 2675-2683
    • Bailey, J.A.1    Tomson, F.L.2    Mecklenburg, S.L.3    MacDonald, G.M.4    Katsonouri, A.5    Puustinen, A.6    Gennis, R.B.7    Woodruff, W.H.8    Dyer, R.B.9
  • 31
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: Electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase
    • A. Kannt, C.R.D. Lancaster, and H. Michel 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.1    Lancaster, C.R.D.2    Michel, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.