메뉴 건너뛰기




Volumn 94, Issue 6, 2008, Pages 2252-2268

Investigations of vibrational coherence in the low-frequency region of ferric heme proteins

Author keywords

[No Author keywords available]

Indexed keywords

HEMOPROTEIN; IRON; LIGAND;

EID: 42149133790     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.122119     Document Type: Article
Times cited : (32)

References (111)
  • 1
    • 0000916745 scopus 로고
    • Femtosecond IR spectroscopy: Methods and applications to protein dynamics
    • Anfinrud, P. A., M. Lim, and T. A. Jackson. 1994. Femtosecond IR spectroscopy: methods and applications to protein dynamics. Proc. SPIE. 2138:107-115.
    • (1994) Proc. SPIE , vol.2138 , pp. 107-115
    • Anfinrud, P.A.1    Lim, M.2    Jackson, T.A.3
  • 3
    • 0019739702 scopus 로고
    • Resonance Raman spectroscopy of hemoglobin
    • Asher, S. 1981. Resonance Raman spectroscopy of hemoglobin. Methods Enzymol. 76:371-413.
    • (1981) Methods Enzymol , vol.76 , pp. 371-413
    • Asher, S.1
  • 5
    • 0034734278 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin
    • Brunori, M. 2000. Structural dynamics of myoglobin. Biophys. Chem. 86:221-230.
    • (2000) Biophys. Chem , vol.86 , pp. 221-230
    • Brunori, M.1
  • 6
  • 7
    • 5644221655 scopus 로고    scopus 로고
    • Rapid timescale processes and the role of electronic surface coupling in the photolysis of diatomic ligands from heme proteins
    • Champion, P. M., F. Rosca, D. Ionascu, W. Cao, and X. Ye. 2004. Rapid timescale processes and the role of electronic surface coupling in the photolysis of diatomic ligands from heme proteins. Faraday Discuss. 127:123-135.
    • (2004) Faraday Discuss , vol.127 , pp. 123-135
    • Champion, P.M.1    Rosca, F.2    Ionascu, D.3    Cao, W.4    Ye, X.5
  • 8
    • 33845281095 scopus 로고
    • Cytochrome.P-450 and chlor-operoxidase-thiolate-ligated heme enzymes-spectroscopic determination of their active-site structures and mechanistic implications of thiolate ligation
    • Dawson, J. H., and M. Sono. 1987. Cytochrome.P-450 and chlor-operoxidase-thiolate-ligated heme enzymes-spectroscopic determination of their active-site structures and mechanistic implications of thiolate ligation. Chem. Rev. 87:1255-1276.
    • (1987) Chem. Rev , vol.87 , pp. 1255-1276
    • Dawson, J.H.1    Sono, M.2
  • 11
    • 0034743152 scopus 로고    scopus 로고
    • Fast protein dynamics probed with infrared vibra-tional echo experiments
    • Fayer, M. D. 2001. Fast protein dynamics probed with infrared vibra-tional echo experiments. Annu. Rev. Phys. Chem. 52:315-356.
    • (2001) Annu. Rev. Phys. Chem , vol.52 , pp. 315-356
    • Fayer, M.D.1
  • 12
    • 0030938807 scopus 로고    scopus 로고
    • On the origin of heme absorption band shifts and associated protein structural relaxation in myoglobin following flash photolysis
    • Franzen, S., and S. G. Boxer. 1997. On the origin of heme absorption band shifts and associated protein structural relaxation in myoglobin following flash photolysis. J. Biol. Chem. 272:9655-9660.
    • (1997) J. Biol. Chem , vol.272 , pp. 9655-9660
    • Franzen, S.1    Boxer, S.G.2
  • 14
    • 0035957014 scopus 로고    scopus 로고
    • The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
    • Frauenfelder, H., B. H. McMahon, R. H. Austin, K. Chu, and J. T. Groves. 2001. The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin. Proc. Natl. Acad. Sci. USA. 98:2370-2374.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2370-2374
    • Frauenfelder, H.1    McMahon, B.H.2    Austin, R.H.3    Chu, K.4    Groves, J.T.5
  • 15
    • 0028308524 scopus 로고
    • Time-resolved resonance Raman spectro-scopy as probe of structure, dynamics, and reactivity in hemoglobin
    • Friedman, J. M. 1994. Time-resolved resonance Raman spectro-scopy as probe of structure, dynamics, and reactivity in hemoglobin. Methods Enzymol. 232:205-231.
    • (1994) Methods Enzymol , vol.232 , pp. 205-231
    • Friedman, J.M.1
  • 16
    • 0000378616 scopus 로고
    • Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation
    • Greene, B. I., R. M. Hochstrasser, R. B. Weisman, and W. A. Eaton. 1978. Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation. Proc. Natl. Acad. Sci. USA. 75:5255-5259.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5255-5259
    • Greene, B.I.1    Hochstrasser, R.M.2    Weisman, R.B.3    Eaton, W.A.4
  • 17
    • 0041179806 scopus 로고
    • Picosecond fluorescence decay of tryptophans in myoglobin
    • Hochstrasser, R. M., and D. K. Negus. 1984. Picosecond fluorescence decay of tryptophans in myoglobin. Proc. Natl. Acad. Sci. USA. 81: 4399-4403.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4399-4403
    • Hochstrasser, R.M.1    Negus, D.K.2
  • 18
    • 0002052550 scopus 로고
    • Heme protein structure and the iron histidine stretching mode
    • Spectro-scopy. T. G. Spiro, editor. Wiley-Interscience, New York, Chichester, Brisbane, Toronto, Singapore
    • Kitagawa, T. 1988. Heme protein structure and the iron histidine stretching mode. In Biological Applications of Raman Spectro-scopy. T. G. Spiro, editor. Wiley-Interscience, New York, Chichester, Brisbane, Toronto, Singapore.
    • (1988) Biological Applications of Raman
    • Kitagawa, T.1
  • 20
    • 58649089172 scopus 로고    scopus 로고
    • Time-resolved infrared studies of ligand dynamics in heme proteins
    • Spectroscopy. M. D. Fayer, editor. Marcel Dekker, New York
    • Lim, M., T. A. Jackson, and P. A. Anfinrud. 2001. Time-resolved infrared studies of ligand dynamics in heme proteins. In Ultrafast Infrared and Raman Spectroscopy. M. D. Fayer, editor. Marcel Dekker, New York.
    • (2001) Ultrafast Infrared and Raman
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 21
    • 0028276741 scopus 로고
    • Femtosecond measurements of geminate recombination in heme- proteins
    • Martin, J. L., and M. H. Vos. 1994. Femtosecond measurements of geminate recombination in heme- proteins. Methods Enzymol. 232: 416-430.
    • (1994) Methods Enzymol , vol.232 , pp. 416-430
    • Martin, J.L.1    Vos, M.H.2
  • 22
    • 0026293863 scopus 로고
    • Vibrational energy relaxation and structural dynamics of heme proteins
    • Miller, R. J. D. 1991. Vibrational energy relaxation and structural dynamics of heme proteins. Annu. Rev. Phys. Chem. 42:581-614.
    • (1991) Annu. Rev. Phys. Chem , vol.42 , pp. 581-614
    • Miller, R.J.D.1
  • 23
    • 0000137291 scopus 로고
    • Energetics and dynamics of deterministic protein motion
    • Miller, R. J. D. 1994. Energetics and dynamics of deterministic protein motion. Acc. Chem. Res. 27:145-150.
    • (1994) Acc. Chem. Res , vol.27 , pp. 145-150
    • Miller, R.J.D.1
  • 24
    • 17044382676 scopus 로고
    • Cytochromes c
    • Springer-Verlag, Berlin, Heidelberg, New York, London, Paris, Tokyo, Hong Kong, Barcelona
    • Moore, G. R., and G. W. Pettigrew. 1990. Cytochromes c. In Evolutionary, Structural and Physicochemical Aspects. Springer-Verlag, Berlin, Heidelberg, New York, London, Paris, Tokyo, Hong Kong, Barcelona.
    • (1990) Evolutionary. Structural and Physicochemical Aspects
    • Moore, G.R.1    Pettigrew, G.W.2
  • 25
    • 0041742184 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Effect of internal cavities on ligand migration and binding
    • Nienhaus, K., P. C. Deng, J. M. Kriegl, and G. U. Nienhaus. 2003. Structural dynamics of myoglobin: Effect of internal cavities on ligand migration and binding. Biochemistry. 42:9647-9658.
    • (2003) Biochemistry , vol.42 , pp. 9647-9658
    • Nienhaus, K.1    Deng, P.C.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 27
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • Olson, J. S., and G. N. Phillips, Jr. 1996. Kinetic pathways and barriers for ligand binding to myoglobin. J. Biol. Chem. 271:17593-17596.
    • (1996) J. Biol. Chem , vol.271 , pp. 17593-17596
    • Olson, J.S.1    Phillips Jr., G.N.2
  • 30
    • 0020972773 scopus 로고
    • Resonance Raman scattering studies of the quaternary structure transition in hemoglobin
    • Rousseau, D. L., and M. R. Ondrias. 1983. Resonance Raman scattering studies of the quaternary structure transition in hemoglobin. Annu. Rev. Biophys. Bioeng. 12:357-380.
    • (1983) Annu. Rev. Biophys. Bioeng , vol.12 , pp. 357-380
    • Rousseau, D.L.1    Ondrias, M.R.2
  • 31
    • 0002179084 scopus 로고
    • Resonance Raman spectroscopy ofmetalloporphyrins
    • Spectros-copy. T. G. Spiro, editor. Wiley-Interscience, New York, Chichester, Brisbane, Toronto, Singapore
    • Spiro, T. G., and H. Y. Li. 1988. Resonance Raman spectroscopy ofmetalloporphyrins. In Biological Applications of Raman Spectros-copy. T. G. Spiro, editor. Wiley-Interscience, New York, Chichester, Brisbane, Toronto, Singapore.
    • (1988) Biological Applications of Raman
    • Spiro, T.G.1    Li, H.Y.2
  • 34
    • 0032964843 scopus 로고    scopus 로고
    • Femtosecond processes in proteins
    • Vos, M. H., and J. L. Martin. 1999. Femtosecond processes in proteins. Biochim. Biophys. Acta. 1411:1-20.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 1-20
    • Vos, M.H.1    Martin, J.L.2
  • 35
    • 0037157156 scopus 로고    scopus 로고
    • 2 and the vibrational relaxation of the six-coordinate heme species
    • 2 and the vibrational relaxation of the six-coordinate heme species. J. Am. Chem. Soc. 124:5914-5924.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 5914-5924
    • Ye, X.1    Demidov, A.2    Champion, P.M.3
  • 36
    • 0035756040 scopus 로고    scopus 로고
    • Ultrafast dynamics of myoglo-bin probed by time-resolved resonance Raman spectroscopy
    • Mizutani, Y., and T. Kitagawa. 2001. Ultrafast dynamics of myoglo-bin probed by time-resolved resonance Raman spectroscopy. Chem. Rec. 1:258-275.
    • (2001) Chem. Rec , vol.1 , pp. 258-275
    • Mizutani, Y.1    Kitagawa, T.2
  • 37
    • 21344439064 scopus 로고    scopus 로고
    • Probing heme protein-ligand interactions by UV/visible absorption spectroscopy
    • Nienhaus, K., and G. U. Nienhaus. 2005. Probing heme protein-ligand interactions by UV/visible absorption spectroscopy. Methods Mol. Biol. 305:215-242.
    • (2005) Methods Mol. Biol , vol.305 , pp. 215-242
    • Nienhaus, K.1    Nienhaus, G.U.2
  • 38
    • 0344730727 scopus 로고
    • Protein fluctuations, distributed coupling, and the binding of ligands to heme-proteins
    • Srajer, V., L. Reinisch, and P. M. Champion. 1988. Protein fluctuations, distributed coupling, and the binding of ligands to heme-proteins. J. Am. Chem. Soc. 110:6656-6670.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 6656-6670
    • Srajer, V.1    Reinisch, L.2    Champion, P.M.3
  • 40
    • 0037038508 scopus 로고    scopus 로고
    • Experimental observation of anharmonic coupling of the heme-doming and iron-ligand out-of-plane vibrational modes confirmed by density functional theory
    • Franzen, S., K. Fritsch, and S. H. Brewer. 2002. Experimental observation of anharmonic coupling of the heme-doming and iron-ligand out-of-plane vibrational modes confirmed by density functional theory. J. Phys. Chem. B. 106:11641-11646.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 11641-11646
    • Franzen, S.1    Fritsch, K.2    Brewer, S.H.3
  • 41
    • 33748480454 scopus 로고    scopus 로고
    • Vibrational assignment and definite harmonic force field for porphine. 2. Comparison with nonresonance Raman data
    • Kozlowski, P. M., A. A. Jarzecki, P. Pulay, X. Y. Li, and M. Z. Zgierski. 1996. Vibrational assignment and definite harmonic force field for porphine. 2. Comparison with nonresonance Raman data. J. Phys. Chem. 100:13985-13992.
    • (1996) J. Phys. Chem , vol.100 , pp. 13985-13992
    • Kozlowski, P.M.1    Jarzecki, A.A.2    Pulay, P.3    Li, X.Y.4    Zgierski, M.Z.5
  • 43
    • 0034319316 scopus 로고    scopus 로고
    • DFT study of structure and vibrations in low-lying spin states of five-coordinated deoxyheme model
    • Kozlowski, P. M., T. G. Spiro, and M. Z. Zgierski. 2000. DFT study of structure and vibrations in low-lying spin states of five-coordinated deoxyheme model. J. Phys. Chem. B. 104:10659-10666.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 10659-10666
    • Kozlowski, P.M.1    Spiro, T.G.2    Zgierski, M.Z.3
  • 44
    • 0002153439 scopus 로고
    • Iron motion in a 5-coordinated heme model
    • Li, X. Y., and M. Z. Zgierski. 1992. Iron motion in a 5-coordinated heme model. Chem. Phys. Lett. 188:16-20.
    • (1992) Chem. Phys. Lett , vol.188 , pp. 16-20
    • Li, X.Y.1    Zgierski, M.Z.2
  • 45
    • 0001540656 scopus 로고    scopus 로고
    • New developments in the calculation of metalloporphyrin Raman spectra via density functional theory
    • Spiro, T. G., P. M. Kozlowski, and M. Z. Zgierski. 1998. New developments in the calculation of metalloporphyrin Raman spectra via density functional theory. J. Raman Spectrosc. 29:869-879.
    • (1998) J. Raman Spectrosc , vol.29 , pp. 869-879
    • Spiro, T.G.1    Kozlowski, P.M.2    Zgierski, M.Z.3
  • 46
    • 0035100895 scopus 로고    scopus 로고
    • Normal-coordinate structural decomposition and the vibronic spectra of porphyrins
    • Shelnutt, J. A. 2001. Normal-coordinate structural decomposition and the vibronic spectra of porphyrins. J. Porphyrins Phthalocyan. 5:300-311.
    • (2001) J. Porphyrins Phthalocyan , vol.5 , pp. 300-311
    • Shelnutt, J.A.1
  • 48
    • 37349001025 scopus 로고    scopus 로고
    • Low-frequency spectral density of ferrous heme: Perturbations induced by axial ligation and protein insertion
    • Gruia, F., X. Ye, D. Ionascu, M. Kubo, and P. Champion. 2007. Low-frequency spectral density of ferrous heme: perturbations induced by axial ligation and protein insertion. Biophys. J. 93:4404-4413.
    • (2007) Biophys. J , vol.93 , pp. 4404-4413
    • Gruia, F.1    Ye, X.2    Ionascu, D.3    Kubo, M.4    Champion, P.5
  • 50
    • 35548977602 scopus 로고    scopus 로고
    • Temperature-dependent heme kinetics: Non-exponential binding and barrier relaxation in the absence of protein conformational substates
    • Ye, X., D. Ionascu, F. Gruia, A. Yu, A. Benabbas, and P. Champion. 2007. Temperature-dependent heme kinetics: non-exponential binding and barrier relaxation in the absence of protein conformational substates. Proc. Natl. Acad. Sci. USA. 104:14682-14687.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14682-14687
    • Ye, X.1    Ionascu, D.2    Gruia, F.3    Yu, A.4    Benabbas, A.5    Champion, P.6
  • 51
    • 0030890923 scopus 로고    scopus 로고
    • Dynamics of cyanide binding to ferrous Scapharca inaequivalvis homodimeric hemoglobin
    • Boffi, A., E. Chiancone, E. S. Peterson, J. Q. Wang, D. L. Rousseau, and J. M. Friedman. 1997. Dynamics of cyanide binding to ferrous Scapharca inaequivalvis homodimeric hemoglobin. Biochemistry. 36:4510-4514.
    • (1997) Biochemistry , vol.36 , pp. 4510-4514
    • Boffi, A.1    Chiancone, E.2    Peterson, E.S.3    Wang, J.Q.4    Rousseau, D.L.5    Friedman, J.M.6
  • 54
    • 0023660146 scopus 로고
    • Recombination of carbon monoxide to ferrous horseradish peroxidase types A and C
    • Doster, W., S. F. Bowne, H. Frauenfelder, L. Reinisch, and E. Shyamsunder. 1987. Recombination of carbon monoxide to ferrous horseradish peroxidase types A and C. J. Mol. Biol. 194:299-312.
    • (1987) J. Mol. Biol , vol.194 , pp. 299-312
    • Doster, W.1    Bowne, S.F.2    Frauenfelder, H.3    Reinisch, L.4    Shyamsunder, E.5
  • 55
    • 0028927331 scopus 로고
    • Evidence for subpicosecond heme doming in hemoglobin and myoglobin-a time-resolved resonance Raman comparison of carbonmonoxy and deoxy species
    • Franzen, S., B. Bohn, C. Poyart, and J. L. Martin. 1995. Evidence for subpicosecond heme doming in hemoglobin and myoglobin-a time-resolved resonance Raman comparison of carbonmonoxy and deoxy species. Biochemistry. 34:1224-1237.
    • (1995) Biochemistry , vol.34 , pp. 1224-1237
    • Franzen, S.1    Bohn, B.2    Poyart, C.3    Martin, J.L.4
  • 56
    • 0035029253 scopus 로고    scopus 로고
    • Heme photolysis occurs by ultrafast excited state metal-to-ring charge transfer
    • Franzen, S., L. Kiger, C. Poyart, and J. L. Martin. 2001. Heme photolysis occurs by ultrafast excited state metal-to-ring charge transfer. Biophys. J. 80:2372-2385.
    • (2001) Biophys. J , vol.80 , pp. 2372-2385
    • Franzen, S.1    Kiger, L.2    Poyart, C.3    Martin, J.L.4
  • 57
    • 0037168603 scopus 로고    scopus 로고
    • Spin-dependent mechanism for diatomic ligand binding to heme
    • Franzen, S. 2002. Spin-dependent mechanism for diatomic ligand binding to heme. Proc. Natl. Acad. Sci. USA. 99:16754-16759.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16754-16759
    • Franzen, S.1
  • 58
    • 0018065699 scopus 로고
    • Principles of ligand binding to heme proteins
    • Frauenfelder, H. 1978. Principles of ligand binding to heme proteins. Methods Enzymol. 54:506-532.
    • (1978) Methods Enzymol , vol.54 , pp. 506-532
    • Frauenfelder, H.1
  • 61
    • 0033522382 scopus 로고    scopus 로고
    • Heme protein dynamics revealed by geminate nitric oxide recombination in mutants of iron and cobalt myoglobin
    • Kholodenko, Y., E. A. Gooding, Y. Dou, M. Ikeda-Saito, and R. M. Hochstrasser. 1999. Heme protein dynamics revealed by geminate nitric oxide recombination in mutants of iron and cobalt myoglobin. Biochemistry. 38:5918-5924.
    • (1999) Biochemistry , vol.38 , pp. 5918-5924
    • Kholodenko, Y.1    Gooding, E.A.2    Dou, Y.3    Ikeda-Saito, M.4    Hochstrasser, R.M.5
  • 62
    • 0019970401 scopus 로고
    • Evidence for hydrogen-bonding of bound dioxy-gen to the distal histidine of oxycobalt myoglobin and hemoglobin
    • Kitagawa, T., M. R. Ondrias, D. L. Rousseau, M. Ikedasaito, and T. Yonetani. 1982. Evidence for hydrogen-bonding of bound dioxy-gen to the distal histidine of oxycobalt myoglobin and hemoglobin. Nature. 298:869-871.
    • (1982) Nature , vol.298 , pp. 869-871
    • Kitagawa, T.1    Ondrias, M.R.2    Rousseau, D.L.3    Ikedasaito, M.4    Yonetani, T.5
  • 63
    • 33845278516 scopus 로고
    • Is bound CO linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data
    • Li, X. Y., and T. G. Spiro. 1988. Is bound CO linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data. J. Am. Chem. Soc. 110:6024-6033.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 6024-6033
    • Li, X.Y.1    Spiro, T.G.2
  • 64
    • 58649094684 scopus 로고
    • Quantic yield of the photo-dissociation of hemoglobin and of myoglobin-kinetic and picosecond spectroscopic analysis
    • Martin, J. L., C. Poyart, A. Migus, and A. Antonetti. 1983. Quantic yield of the photo-dissociation of hemoglobin and of myoglobin-kinetic and picosecond spectroscopic analysis. Nouv. Rev. Fr. Hematol 25:44-45.
    • (1983) Nouv. Rev. Fr. Hematol , vol.25 , pp. 44-45
    • Martin, J.L.1    Poyart, C.2    Migus, A.3    Antonetti, A.4
  • 65
    • 0030773396 scopus 로고    scopus 로고
    • 2, NO, and CO by electrostatic interactions with the bound ligand. J. Biol. Inorg. Chem. 2:544-552.
    • 2, NO, and CO by electrostatic interactions with the bound ligand. J. Biol. Inorg. Chem. 2:544-552.
  • 67
    • 0039158100 scopus 로고    scopus 로고
    • Dynamics of carbon monoxide binding with cytochromes P-450
    • Tetreau, C., C. Diprimo, R. Lange, H. Tourbez, and D. Lavalette. 1997. Dynamics of carbon monoxide binding with cytochromes P-450. Biochemistry. 36:10262-10275.
    • (1997) Biochemistry , vol.36 , pp. 10262-10275
    • Tetreau, C.1    Diprimo, C.2    Lange, R.3    Tourbez, H.4    Lavalette, D.5
  • 68
    • 17744362896 scopus 로고    scopus 로고
    • CO rebinding to protoheme: Investigations of the proximal and distal contributions to the geminate rebinding barrier
    • Ye, X., A. Yu, G. Y. Georgiev, F. Gruia, D. Ionascu, W. Cao, J. T. Sage, and P. M. Champion. 2005. CO rebinding to protoheme: investigations of the proximal and distal contributions to the geminate rebinding barrier. J. Am. Chem. Soc. 127:5854-5861.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 5854-5861
    • Ye, X.1    Yu, A.2    Georgiev, G.Y.3    Gruia, F.4    Ionascu, D.5    Cao, W.6    Sage, J.T.7    Champion, P.M.8
  • 70
    • 0001220593 scopus 로고    scopus 로고
    • Anharmonic protein motions and heme deformations in myoglobin cyanide probed by absorption and resonance Raman spectroscopy
    • Schweitzer-Stenner, R., A. Cupane, M. Leone, C. Lemke, J. Schott, and W. Dreybrodt. 2000. Anharmonic protein motions and heme deformations in myoglobin cyanide probed by absorption and resonance Raman spectroscopy. J. Phys. Chem. B. 104:4754-4764.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4754-4764
    • Schweitzer-Stenner, R.1    Cupane, A.2    Leone, M.3    Lemke, C.4    Schott, J.5    Dreybrodt, W.6
  • 71
    • 0021989717 scopus 로고
    • Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites
    • Yoshikawa, S., D. H. O'Keeffe, and W. S. Caughey. 1985. Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites. J. Biol. Chem. 260:3518-3528.
    • (1985) J. Biol. Chem , vol.260 , pp. 3518-3528
    • Yoshikawa, S.1    O'Keeffe, D.H.2    Caughey, W.S.3
  • 72
    • 0025303661 scopus 로고
    • Infrared evidence of cyanide binding to iron and copper sites in bovine heart cytochrome c oxidase. Implications regarding oxygen reduction
    • Yoshikawa, S., and W. S. Caughey. 1990. Infrared evidence of cyanide binding to iron and copper sites in bovine heart cytochrome c oxidase. Implications regarding oxygen reduction. J. Biol. Chem. 265: 7945-7958.
    • (1990) J. Biol. Chem , vol.265 , pp. 7945-7958
    • Yoshikawa, S.1    Caughey, W.S.2
  • 73
    • 33847151331 scopus 로고    scopus 로고
    • Energetics and dynamics in MbCN:CN(-)-vibrational relaxation from molecular dynamics simulations
    • Danielsson, J. and M. Meuwly. 2007. Energetics and dynamics in MbCN:CN(-)-vibrational relaxation from molecular dynamics simulations. J. Phys. Chem. B. 111:218-226.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 218-226
    • Danielsson, J.1    Meuwly, M.2
  • 74
    • 0001677013 scopus 로고
    • Femtosecond laser observations of molecular vibration and rotation
    • Dantus, M., R. M. Bowman, and A. H. Zewail. 1990. Femtosecond laser observations of molecular vibration and rotation. Nature. 343: 737-739.
    • (1990) Nature , vol.343 , pp. 737-739
    • Dantus, M.1    Bowman, R.M.2    Zewail, A.H.3
  • 76
    • 33751157106 scopus 로고
    • Femtosecond wavepacket spectroscopy-influence of temperature, wavelength, and pulse duration
    • Jonas, D. M., S. E. Bradforth, S. A. Passino, and G. R. Fleming. 1995. Femtosecond wavepacket spectroscopy-influence of temperature, wavelength, and pulse duration. J. Phys. Chem. 99:2594-2608.
    • (1995) J. Phys. Chem , vol.99 , pp. 2594-2608
    • Jonas, D.M.1    Bradforth, S.E.2    Passino, S.A.3    Fleming, G.R.4
  • 77
    • 0035121238 scopus 로고    scopus 로고
    • Investigations of amplitude and phase excitation profiles in femtosecond coherence spectroscopy
    • Kumar, A. T. N., F. Rosca, A. Widom, and P. M. Champion. 2001. Investigations of amplitude and phase excitation profiles in femtosecond coherence spectroscopy. J. Chem. Phys. 114:701-724.
    • (2001) J. Chem. Phys , vol.114 , pp. 701-724
    • Kumar, A.T.N.1    Rosca, F.2    Widom, A.3    Champion, P.M.4
  • 78
    • 0035870565 scopus 로고    scopus 로고
    • Investigations of ultrafast nuclear response induced by resonant and nonresonant laser pulses
    • Kumar, A. T. N., F. Rosca, A. Widom, and P. M. Champion. 2001. Investigations of ultrafast nuclear response induced by resonant and nonresonant laser pulses. J. Chem. Phys. 114:6795-6815.
    • (2001) J. Chem. Phys , vol.114 , pp. 6795-6815
    • Kumar, A.T.N.1    Rosca, F.2    Widom, A.3    Champion, P.M.4
  • 79
    • 0002924146 scopus 로고
    • Femtosecond optical spectroscopy-a direct look at elementary chemical events
    • Mukamel, S. 1990. Femtosecond optical spectroscopy-a direct look at elementary chemical events. Annu. Rev. Phys. Chem. 41:647-681.
    • (1990) Annu. Rev. Phys. Chem , vol.41 , pp. 647-681
    • Mukamel, S.1
  • 80
    • 85050201686 scopus 로고
    • Femtosecond coherent spectroscopy
    • Nelson, K. A., and E. P. Ippen. 1989. Femtosecond coherent spectroscopy. Adv. Chem. Phys. 75:1-35.
    • (1989) Adv. Chem. Phys , vol.75 , pp. 1-35
    • Nelson, K.A.1    Ippen, E.P.2
  • 81
    • 0031210745 scopus 로고    scopus 로고
    • A multidimensional Landau-Zener description of chemical reaction dynamics and vibrational coherence
    • Zhu, L. Y., A. Widom, and P. M. Champion. 1997. A multidimensional Landau-Zener description of chemical reaction dynamics and vibrational coherence. J. Chem. Phys. 107:2859-2871.
    • (1997) J. Chem. Phys , vol.107 , pp. 2859-2871
    • Zhu, L.Y.1    Widom, A.2    Champion, P.M.3
  • 82
    • 36449006690 scopus 로고
    • Femtosecond polarization spectroscopy - a density-matrix description
    • Ziegler, L. D., R. Fan, A. E. Desrosiers, and N. F. Scherer. 1994. Femtosecond polarization spectroscopy - a density-matrix description. J. Chem. Phys. 100:1823-1839.
    • (1994) J. Chem. Phys , vol.100 , pp. 1823-1839
    • Ziegler, L.D.1    Fan, R.2    Desrosiers, A.E.3    Scherer, N.F.4
  • 83
    • 33847799938 scopus 로고
    • Fluorescence, resonance Raman, and radiationless decay in several hemoproteins
    • Adar, F., M. Gouterman, and S. Aronowitz. 1976. Fluorescence, resonance Raman, and radiationless decay in several hemoproteins. J. Phys. Chem. 80:2184-2191.
    • (1976) J. Phys. Chem , vol.80 , pp. 2184-2191
    • Adar, F.1    Gouterman, M.2    Aronowitz, S.3
  • 84
    • 0000167360 scopus 로고
    • On the quantitation of light emission from cytochrome c in the low quantum yield limit
    • Champion, P., and R. Lange. 1980. On the quantitation of light emission from cytochrome c in the low quantum yield limit. J. Chem. Phys. 73:5947-5957.
    • (1980) J. Chem. Phys , vol.73 , pp. 5947-5957
    • Champion, P.1    Lange, R.2
  • 85
    • 0000839865 scopus 로고
    • Observation and quantitation of light emission from cytochrome c using Soret band laser excitation
    • Champion, P., and G. J. Perreault. 1981. Observation and quantitation of light emission from cytochrome c using Soret band laser excitation. J. Chem. Phys. 75:490-491.
    • (1981) J. Chem. Phys , vol.75 , pp. 490-491
    • Champion, P.1    Perreault, G.J.2
  • 86
    • 0011478446 scopus 로고
    • Excited state lifetimes in cytochromes measured from Raman scattering data: Evidence for iron-porphyrin interactions
    • Friedman, J. M., D. L. Rousseau, and F. Adar. 1977. Excited state lifetimes in cytochromes measured from Raman scattering data: evidence for iron-porphyrin interactions. Proc. Natl. Acad. Sci. USA. 74:2607-2611.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2607-2611
    • Friedman, J.M.1    Rousseau, D.L.2    Adar, F.3
  • 87
    • 0040464327 scopus 로고
    • Probes of structure and function of macromolecules and membranes
    • B. Chance, C. Lee, and J. Blaise, editors. Academic Press, New York
    • Hochstrasser, R. M. 1971. Probes of structure and function of macromolecules and membranes. In Probes of Structure and Function of Macromolecules and Membranes. B. Chance, C. Lee, and J. Blaise, editors. Academic Press, New York.
    • (1971) Probes of Structure and Function of Macromolecules and Membranes
    • Hochstrasser, R.M.1
  • 88
    • 1542305690 scopus 로고    scopus 로고
    • Dynamic absorption spectral contours: Vibrational phase-dependent resolution of low frequency coherent wave packet motion of IR144 on the ground state and excited state surfaces
    • Carson, E. A., W. M. Diffey, K. R. Shelly, S. Lampa-Pastirk, K. L. Dillman, J. M. Schleicher, and W. F. Beck. 2004. Dynamic absorption spectral contours: vibrational phase-dependent resolution of low frequency coherent wave packet motion of IR144 on the ground state and excited state surfaces. J. Phys. Chem. 108:1489-1500.
    • (2004) J. Phys. Chem , vol.108 , pp. 1489-1500
    • Carson, E.A.1    Diffey, W.M.2    Shelly, K.R.3    Lampa-Pastirk, S.4    Dillman, K.L.5    Schleicher, J.M.6    Beck, W.F.7
  • 92
    • 0035899723 scopus 로고    scopus 로고
    • On the rate distribution analysis of kinetics data using the maximum entropy method: Application to myoglobin relaxation on the nanosecond and femtosecond timescales
    • Kumar, A. T. N., L. Zhu, J. F. Christian, A. A. Demidov, and P. M. Champion. 2001. On the rate distribution analysis of kinetics data using the maximum entropy method: application to myoglobin relaxation on the nanosecond and femtosecond timescales. J. Phys. Chem. B. 105:7847-7856.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7847-7856
    • Kumar, A.T.N.1    Zhu, L.2    Christian, J.F.3    Demidov, A.A.4    Champion, P.M.5
  • 93
    • 4243376461 scopus 로고
    • Photochemical breakage ofMbCO through UV illumination
    • Bucher, T., and J. Kaspers. 1947. Photochemical breakage ofMbCO through UV illumination. Biochim. Biophys. Acta. 1:21-34.
    • (1947) Biochim. Biophys. Acta , vol.1 , pp. 21-34
    • Bucher, T.1    Kaspers, J.2
  • 94
    • 0018024764 scopus 로고
    • Carboxylation kinetics of hemoglobin and myoglobin: Linear transient response to step perturbation by laser photolysis
    • Schuresko, D. D., and W. W. Webb. 1978. Carboxylation kinetics of hemoglobin and myoglobin: linear transient response to step perturbation by laser photolysis. Biophys. J. 24:382-383.
    • (1978) Biophys. J , vol.24 , pp. 382-383
    • Schuresko, D.D.1    Webb, W.W.2
  • 95
    • 0030467166 scopus 로고    scopus 로고
    • Assignment ofprotoheme resonance Raman spectrum by heme labeling in myoglobin
    • Hu, S., K. M. Smith, and T. G. Spiro. 1996. Assignment ofprotoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118:12638-12646.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 96
    • 10744221411 scopus 로고    scopus 로고
    • Investigations of heme protein absorption lineshapes, vibrational relaxation, and resonance Raman scattering on ultrafast timescales
    • Ye, X., A. Demidov, F. Rosca, W. Wang, A. Kumar, D. Ionascu, L. Zhu, D. Barrick, D. Wharton, and P. M. Champion. 2003. Investigations of heme protein absorption lineshapes, vibrational relaxation, and resonance Raman scattering on ultrafast timescales. J. Phys. Chem. A. 107:8156-8165.
    • (2003) J. Phys. Chem. A , vol.107 , pp. 8156-8165
    • Ye, X.1    Demidov, A.2    Rosca, F.3    Wang, W.4    Kumar, A.5    Ionascu, D.6    Zhu, L.7    Barrick, D.8    Wharton, D.9    Champion, P.M.10
  • 97
    • 0000988407 scopus 로고
    • Resonance Raman-scattering as a probe of electron nuclear coupling-applications to heme-proteins
    • Morikis, D., P. Li, O. Bangcharoenpaurpong, J. T. Sage, and P. M. Champion. 1991. Resonance Raman-scattering as a probe of electron nuclear coupling-applications to heme-proteins. J. Phys. Chem. 95: 3391-3398.
    • (1991) J. Phys. Chem , vol.95 , pp. 3391-3398
    • Morikis, D.1    Li, P.2    Bangcharoenpaurpong, O.3    Sage, J.T.4    Champion, P.M.5
  • 98
    • 0024278596 scopus 로고    scopus 로고
    • Jongeward,K.A.,D.Magde,D.J.Taube,and T.G.Traylor.1988.Pico-second kinetics of cytochromes b5and c. J. Biol. Chem. 263:6027-6030.
    • Jongeward,K.A.,D.Magde,D.J.Taube,and T.G.Traylor.1988.Pico-second kinetics of cytochromes b5and c. J. Biol. Chem. 263:6027-6030.
  • 99
    • 7444256720 scopus 로고    scopus 로고
    • Photodissociation of heme distal methionine in ferrous cyto-chrome c revealed by subpicosecond time-resolved resonance Raman spectroscopy
    • Cianetti, S., M. Negrerie, M. H. Vos, J. L. Martin, and S. G. Kruglik. 2004. Photodissociation of heme distal methionine in ferrous cyto-chrome c revealed by subpicosecond time-resolved resonance Raman spectroscopy. J. Am. Chem. Soc. 126:13932-13933.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 13932-13933
    • Cianetti, S.1    Negrerie, M.2    Vos, M.H.3    Martin, J.L.4    Kruglik, S.G.5
  • 100
    • 0022961088 scopus 로고
    • Molecular dynamics simulations of cooling in laser-excited heme proteins
    • Henry, E. R., W. A. Eaton, and R. M. Hochstrasser. 1986. Molecular dynamics simulations of cooling in laser-excited heme proteins. Proc. Natl. Acad. Sci. USA. 83:8982-8986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8982-8986
    • Henry, E.R.1    Eaton, W.A.2    Hochstrasser, R.M.3
  • 101
    • 85031358822 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 102
    • 0030689835 scopus 로고    scopus 로고
    • Direct observation of cooling of heme upon photodissociation of carbonmonoxy myoglobin
    • Mizutani, Y., and T. Kitagawa. 1997. Direct observation of cooling of heme upon photodissociation of carbonmonoxy myoglobin. Science. 278:443-446.
    • (1997) Science , vol.278 , pp. 443-446
    • Mizutani, Y.1    Kitagawa, T.2
  • 103
    • 0001614405 scopus 로고    scopus 로고
    • Intramolecular vibrational energy redistribution and intermolecular energy transfer in the (d, d) excited state of nickel octaethylporphyrin
    • Mizutani, Y., Y. Uesuggi, and T. Kitagawa. 1999. Intramolecular vibrational energy redistribution and intermolecular energy transfer in the (d, d) excited state of nickel octaethylporphyrin. J. Chem. Phys. 111:8950-8962.
    • (1999) J. Chem. Phys , vol.111 , pp. 8950-8962
    • Mizutani, Y.1    Uesuggi, Y.2    Kitagawa, T.3
  • 104
    • 0001434099 scopus 로고
    • Proton nuclear magnetic resonance study of the relaxation behavior and kinetic lability of exchangeable protons in the heme pocket of cyanomet-myoglobin
    • Cutnell, J. D., G. N. La Mar, and S. B. Kong. 1981. Proton nuclear magnetic resonance study of the relaxation behavior and kinetic lability of exchangeable protons in the heme pocket of cyanomet-myoglobin. J. Am. Chem. Soc. 103:3567-3572.
    • (1981) J. Am. Chem. Soc , vol.103 , pp. 3567-3572
    • Cutnell, J.D.1    La Mar, G.N.2    Kong, S.B.3
  • 105
    • 0032975875 scopus 로고    scopus 로고
    • A study of vibrational relaxation of B-state carbon monoxide in the heme pocket of photolyzed carboxymyoglobin
    • Sagnella, D. E., and J. E. Straub. 1999. A study of vibrational relaxation of B-state carbon monoxide in the heme pocket of photolyzed carboxymyoglobin. Biophys. J. 77:70-84.
    • (1999) Biophys. J , vol.77 , pp. 70-84
    • Sagnella, D.E.1    Straub, J.E.2
  • 106
    • 0027368854 scopus 로고
    • High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin
    • Quillin, M. L., R. M. Arduini, J. S. Olson, and G. N. Phillips, Jr. 1993. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J. Mol. Biol. 234:140-155.
    • (1993) J. Mol. Biol , vol.234 , pp. 140-155
    • Quillin, M.L.1    Arduini, R.M.2    Olson, J.S.3    Phillips Jr., G.N.4
  • 108
    • 0030197801 scopus 로고    scopus 로고
    • Femtosecond near-IR absorbance study of photoexcited myoglobin: Dynamics of electronic and thermal relaxation
    • Lim, M. H., T. A. Jackson, and P. A. Anfinrud. 1996. Femtosecond near-IR absorbance study of photoexcited myoglobin: dynamics of electronic and thermal relaxation. J. Phys. Chem. 100:12043-12051.
    • (1996) J. Phys. Chem , vol.100 , pp. 12043-12051
    • Lim, M.H.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 110
    • 85031359894 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 111
    • 0000777551 scopus 로고
    • Investigations of spectral broadening mechanisms in biomolecules: Cytochrome-c
    • Schomacker, K. T., and P. M. Champion. 1986. Investigations of spectral broadening mechanisms in biomolecules: cytochrome-c. J. Chem. Phys. 84:5314-5325.
    • (1986) J. Chem. Phys , vol.84 , pp. 5314-5325
    • Schomacker, K.T.1    Champion, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.