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Volumn 401, Issue 6749, 1999, Pages 181-184

Coherent reaction dynamics in a bacterial cytochrome c oxidase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME C OXIDASE; LIGAND;

EID: 0033539117     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/43699     Document Type: Article
Times cited : (90)

References (30)
  • 1
    • 0000419823 scopus 로고
    • Visualization of coherent nuclear motion in a membrane protein by femtosecond spectroscopy
    • Vos, M. H., Rappaport, F., Lambry, J.-C., Breton, J. & Martin, J.-L. Visualization of coherent nuclear motion in a membrane protein by femtosecond spectroscopy. Nature 363, 320-325 (1993).
    • (1993) Nature , vol.363 , pp. 320-325
    • Vos, M.H.1    Rappaport, F.2    Lambry, J.-C.3    Breton, J.4    Martin, J.-L.5
  • 2
    • 0028519152 scopus 로고
    • Vibrationally coherent photochemistry in the femtosecond primary event of vision
    • Wang, Q., Schoenlein, R. W., Peteanu, L. A., Mathies, R. A. & Shank, C. V. Vibrationally coherent photochemistry in the femtosecond primary event of vision. Science 266, 422-424 (1994).
    • (1994) Science , vol.266 , pp. 422-424
    • Wang, Q.1    Schoenlein, R.W.2    Peteanu, L.A.3    Mathies, R.A.4    Shank, C.V.5
  • 3
    • 0028519187 scopus 로고
    • Observation of coherent reaction dynamics in heme proteins
    • Zhu, L., Sage, J. T. & Champion, P. M. Observation of coherent reaction dynamics in heme proteins. Science 266, 629-632 (1994).
    • (1994) Science , vol.266 , pp. 629-632
    • Zhu, L.1    Sage, J.T.2    Champion, P.M.3
  • 4
    • 0025995721 scopus 로고
    • Direct observation of vibrational coherence in bacterial reaction centers using femtosecond absorption spectroscopy
    • Vos, M. H. et al. Direct observation of vibrational coherence in bacterial reaction centers using femtosecond absorption spectroscopy. Proc Natl Acad. Sci. USA 88, 8885-8889 (1991).
    • (1991) Proc Natl Acad. Sci. USA , vol.88 , pp. 8885-8889
    • Vos, M.H.1
  • 5
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock, G. T. & Wikström, M. Oxygen activation and the conservation of energy in cell respiration. Nature 356, 301-309 (1992).
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 6
    • 0027359220 scopus 로고
    • The gateway to the active site of heme-copper oxidases
    • Lemon, D. D., Calhoun, M. W., Gennis, R. B. & Woodruff, W. H. The gateway to the active site of heme-copper oxidases. Biochemistry 32, 11953-11956 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11953-11956
    • Lemon, D.D.1    Calhoun, M.W.2    Gennis, R.B.3    Woodruff, W.H.4
  • 7
    • 0028210150 scopus 로고
    • Oxygen binding and activation: Early steps in the reaction of oxygen with cytochrome c oxidase
    • Verkhovsky, M. I., Morgan, J. E. & Wikström, M. Oxygen binding and activation: early steps in the reaction of oxygen with cytochrome c oxidase. Biochemistry 33, 3079-3086 (1994).
    • (1994) Biochemistry , vol.33 , pp. 3079-3086
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 8
    • 0028013676 scopus 로고
    • Picosecond infrared study of the photodynamics of carbonmonoxy-cytochrome c oxidase
    • Dyer, R. B., Peterson, K. A., Stoutland, P. O. & Woodruff, W. H. Picosecond infrared study of the photodynamics of carbonmonoxy-cytochrome c oxidase. Biochemistry 33, 500-507 (1994).
    • (1994) Biochemistry , vol.33 , pp. 500-507
    • Dyer, R.B.1    Peterson, K.A.2    Stoutland, P.O.3    Woodruff, W.H.4
  • 10
    • 33751499747 scopus 로고
    • Femtosecond dynamics of reduced cytochrome c oxidase and its CO derivative
    • Stoutland, P. O., Lambry, J.-C., Martin, J.-L. & Woodruff, W. H. Femtosecond dynamics of reduced cytochrome c oxidase and its CO derivative. J. Phys. Chem. 95, 6406-6408 (1991).
    • (1991) J. Phys. Chem. , vol.95 , pp. 6406-6408
    • Stoutland, P.O.1    Lambry, J.-C.2    Martin, J.-L.3    Woodruff, W.H.4
  • 11
    • 0013889222 scopus 로고
    • 3 in cytochrome c oxidase
    • 3 in cytochrome c oxidase. Biochemistry 5, 838-848 (1966).
    • (1966) Biochemistry , vol.5 , pp. 838-848
    • Vanneste, W.H.1
  • 12
    • 0032361412 scopus 로고    scopus 로고
    • Vibrational coherence in bacterial reaction centers: Spectroscopic characterisation of motions active during primary electron transfer
    • Vos, M. H., Jones, M. R. & Martin, J.-L. Vibrational coherence in bacterial reaction centers: spectroscopic characterisation of motions active during primary electron transfer. Chem. Phys. 233, 179-190 (1998).
    • (1998) Chem. Phys. , vol.233 , pp. 179-190
    • Vos, M.H.1    Jones, M.R.2    Martin, J.-L.3
  • 13
    • 0028021633 scopus 로고
    • Time-resolved optical absorption studies of intramolecular electron transfer in cytochrome c oxidase
    • Georgiadis, K. E., Jhon, N.-I. & Einarsdóttir, Ó. Time-resolved optical absorption studies of intramolecular electron transfer in cytochrome c oxidase. Biochemistry 33, 9245-9256 (1994).
    • (1994) Biochemistry , vol.33 , pp. 9245-9256
    • Georgiadis, K.E.1    Jhon, N.-I.2    Einarsdóttir, Ó.3
  • 14
    • 0004198783 scopus 로고
    • (eds Auston, D. H. & Eisenthal, K. B.) Springer, Berlin
    • Martin, J.-L. et al. in Ultrafast Phenomenon IV (eds Auston, D. H. & Eisenthal, K. B.) 447-451 (Springer, Berlin, 1984).
    • (1984) Ultrafast Phenomenon IV , pp. 447-451
    • Martin, J.-L.1
  • 15
    • 0001807834 scopus 로고
    • Dynamics of activationless reactions in solution
    • Bagchi, B. & Fleming, G. R. Dynamics of activationless reactions in solution. J. Phys. Chem. 94, 9-20 (1990).
    • (1990) J. Phys. Chem. , vol.94 , pp. 9-20
    • Bagchi, B.1    Fleming, G.R.2
  • 16
    • 0028408155 scopus 로고
    • Direct evidence for the role of haem doming as the primary event in the cooperative transition of haemoglobin
    • Franzen, S., Lambry, J.-C., Bohn, B., Poyart, C. & Martin, J.-L. Direct evidence for the role of haem doming as the primary event in the cooperative transition of haemoglobin. Nature Struct. Biol. 1, 230-233 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 230-233
    • Franzen, S.1    Lambry, J.-C.2    Bohn, B.3    Poyart, C.4    Martin, J.-L.5
  • 17
    • 0002153439 scopus 로고
    • Iron motion in a five-coordinated heme model
    • Li, X.-Y. & Zgierski, M. Z. Iron motion in a five-coordinated heme model. Chem. Phys. Lett. 188, 16-20 (1992).
    • (1992) Chem. Phys. Lett. , vol.188 , pp. 16-20
    • Li, X.-Y.1    Zgierski, M.Z.2
  • 19
    • 18144447465 scopus 로고    scopus 로고
    • Redox-coupled structure changes in bovine heart cytochrome c oxidase
    • Yoshikawa, S. et al. Redox-coupled structure changes in bovine heart cytochrome c oxidase. Science 280, 1723-1729 (1998).
    • (1998) Science , vol.280 , pp. 1723-1729
    • Yoshikawa, S.1
  • 21
    • 0031054657 scopus 로고    scopus 로고
    • Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin
    • Lim, M., Jackson, T. A. & Anfinrud, P. A. Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin. Nature Struct. Boil. 4, 209-214 (1997).
    • (1997) Nature Struct. Boil. , vol.4 , pp. 209-214
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 22
    • 0031553385 scopus 로고    scopus 로고
    • Femtosecond time-resolved X-ray diffraction from laser-heated organic films
    • Rischel, C. et al. Femtosecond time-resolved X-ray diffraction from laser-heated organic films. Nature 390, 490-492 (1997).
    • (1997) Nature , vol.390 , pp. 490-492
    • Rischel, C.1
  • 23
    • 0022821996 scopus 로고
    • Cytochrome c oxidase from Paracoccus denitrificans
    • Ludwig, B. Cytochrome c oxidase from Paracoccus denitrificans. Meth. Enzymol. 126, 153-159 (1986).
    • (1986) Meth. Enzymol. , vol.126 , pp. 153-159
    • Ludwig, B.1
  • 24
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans
    • Haltia, T., Semo, N., Arrondo, J. L. R., Goñi, F. M. & Freire, E. Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 33, 9731-9740 (1994).
    • (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
  • 25
    • 0028276741 scopus 로고
    • Femtosecond measurements of geminate recombination in heme proteins
    • Martin, J.-L. & Vos, M. H. Femtosecond measurements of geminate recombination in heme proteins. Methods Enzymol. 232, 416-430 (1994).
    • (1994) Methods Enzymol. , vol.232 , pp. 416-430
    • Martin, J.-L.1    Vos, M.H.2
  • 26
    • 0019739702 scopus 로고
    • Resonance Raman spectroscopy of hemoglobin
    • Asher, S. Resonance Raman spectroscopy of hemoglobin. Methods Enzymol. 76, 371-413 (1981).
    • (1981) Methods Enzymol. , vol.76 , pp. 371-413
    • Asher, S.1
  • 27
    • 0032514692 scopus 로고    scopus 로고
    • Low-frequency vibrational modes in proteins: Changes induced by point-mutations in the protein-cofactor matrix of bacterial reaction centers
    • Rischel, C. et al. Low-frequency vibrational modes in proteins: changes induced by point-mutations in the protein-cofactor matrix of bacterial reaction centers. Proc. Natl Acad. Sci. USA 95, 12306-12311 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12306-12311
    • Rischel, C.1
  • 28
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D - Photorealistic molecular graphics
    • Merritt, E. A. & Bacon, D. J. Raster3D - photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.