메뉴 건너뛰기




Volumn 24, Issue 3, 1996, Pages 117-124

Low temperature optical spectroscopy of low-spin ferric hemeproteins

Author keywords

optical spectroscopy; protein dynamics

Indexed keywords

HEMOGLOBIN; MYOGLOBIN;

EID: 0030061303     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00180268     Document Type: Article
Times cited : (6)

References (37)
  • 2
    • 0019739702 scopus 로고
    • Resonance Raman spectroscopy of hemoglobin
    • Asher SA (1981) Resonance Raman spectroscopy of hemoglobin. Methods Enzymol 76:371-413
    • (1981) Methods Enzymol , vol.76 , pp. 371-413
    • Asher, S.A.1
  • 4
    • 0028133298 scopus 로고
    • Ligand binding kinetics and optical absorption spectra in the cooperative homodimeric scapharca inaequivalvis hemoglobin. Effect of protein fluctuations
    • Boffi A, Verzili D, Chiancone E, Leone M, Cupane A, Militello V, Vitrano E, Cordone L, Yu W, Di Iorio EE (1994) Ligand binding kinetics and optical absorption spectra in the cooperative homodimeric scapharca inaequivalvis hemoglobin. Effect of protein fluctuations. Biophys J 67:1713-1723
    • (1994) Biophys J , vol.67 , pp. 1713-1723
    • Boffi, A.1    Verzili, D.2    Chiancone, E.3    Leone, M.4    Cupane, A.5    Militello, V.6    Vitrano, E.7    Cordone, L.8    Yu, W.9    Di Iorio, E.E.10
  • 5
    • 0001374378 scopus 로고
    • Temperature effects in the time correlator theory of resonance raman scattering
    • Chan CK, Page JB (1983) Temperature effects in the time correlator theory of resonance raman scattering. J Chem Phys 79: 5234-5250
    • (1983) J Chem Phys , vol.79 , pp. 5234-5250
    • Chan, C.K.1    Page, J.B.2
  • 6
    • 0018650340 scopus 로고
    • Effect of some monohydric alcohols on the oxygen affinity of hemoglobin: Relevance of solvent dielectric constant and hydrophobicity
    • Cordone L, Cupane A, San Biagio PL, Vitrano E (1979) Effect of some monohydric alcohols on the oxygen affinity of hemoglobin: relevance of solvent dielectric constant and hydrophobicity. Biopolymers 18:1975-1988
    • (1979) Biopolymers , vol.18 , pp. 1975-1988
    • Cordone, L.1    Cupane, A.2    San Biagio, P.L.3    Vitrano, E.4
  • 7
    • 0022467258 scopus 로고
    • Optical absorption spectra of deoxy- and oxyhemoglobin in the temperature range 300-20 K: Relation with protein dynamics
    • Cordone L, Cupane A, Leone M, Vitrano E (1986) Optical absorption spectra of deoxy- and oxyhemoglobin in the temperature range 300-20 K: relation with protein dynamics. Biophys Chem 24:259-275
    • (1986) Biophys Chem , vol.24 , pp. 259-275
    • Cordone, L.1    Cupane, A.2    Leone, M.3    Vitrano, E.4
  • 8
    • 0023898888 scopus 로고
    • Interaction between external medium and haem pocket in myoglobin probed by low-temperature optical specroscopy
    • Cordone L, Cupane A, Leone M, Vitrano E, Bulone D (1988) Interaction between external medium and haem pocket in myoglobin probed by low-temperature optical specroscopy. J Mol Biol 198:213-218
    • (1988) J Mol Biol , vol.198 , pp. 213-218
    • Cordone, L.1    Cupane, A.2    Leone, M.3    Vitrano, E.4    Bulone, D.5
  • 9
    • 0025219483 scopus 로고
    • Thermal behaviour of the 760 nm absorption band in photodissociated sperm whale carbonmonoxy-myoglobin at cryogenic temperature: Dependence on external medium
    • Cordone L, Cupane A, Leone M, Vitrano E (1990) Thermal behaviour of the 760 nm absorption band in photodissociated sperm whale carbonmonoxy-myoglobin at cryogenic temperature: dependence on external medium. Biopolymers 29:639-643
    • (1990) Biopolymers , vol.29 , pp. 639-643
    • Cordone, L.1    Cupane, A.2    Leone, M.3    Vitrano, E.4
  • 11
    • 0024208880 scopus 로고
    • Structural and dynamic properties of the heme pocket in myoglobin probes by optical spectroscopy
    • Cupane A, Leone M, Vitrano E, Cordone L (1988) Structural and dynamic properties of the heme pocket in myoglobin probes by optical spectroscopy. Biopolymers 27:1977-1997
    • (1988) Biopolymers , vol.27 , pp. 1977-1997
    • Cupane, A.1    Leone, M.2    Vitrano, E.3    Cordone, L.4
  • 12
    • 0027401649 scopus 로고
    • Protein dynamics: Conformational disorder, vibrational coupling and anharmonicity in deoxyhemoglobin and myoglobin
    • Cupane A, Leone M, Vitrano E (1993a) Protein dynamics: conformational disorder, vibrational coupling and anharmonicity in deoxyhemoglobin and myoglobin. Eur Biophys J 21:385-391
    • (1993) Eur Biophys J , vol.21 , pp. 385-391
    • Cupane, A.1    Leone, M.2    Vitrano, E.3
  • 13
    • 0027137933 scopus 로고
    • Structure-dynamics-function relationships in Asian Elephant (Elephas maximus) myoglobin. An optical spectroscopy and flash-photolysis study on functionally important motions
    • Cupane A, Leone M, Vitrano E, Cordone L, Hiltpold UR, Winterhalter KH, Yu W, Di Iorio EE (1993b) Structure-dynamics-function relationships in Asian Elephant (Elephas maximus) myoglobin. An optical spectroscopy and flash-photolysis study on functionally important motions. Biophys J 65:2461-2472
    • (1993) Biophys J , vol.65 , pp. 2461-2472
    • Cupane, A.1    Leone, M.2    Vitrano, E.3    Cordone, L.4    Hiltpold, U.R.5    Winterhalter, K.H.6    Yu, W.7    Di Iorio, E.E.8
  • 14
    • 0028922168 scopus 로고
    • Low temperature optical absorption spectroscopy: An approach to the study of stereodynamic properties of hemeproteins
    • Cupane A, Leone M, Vitrano E, Cordone L (1995) Low temperature optical absorption spectroscopy: an approach to the study of stereodynamic properties of hemeproteins. Eur Biophys J 23:385-398
    • (1995) Eur Biophys J , vol.23 , pp. 385-398
    • Cupane, A.1    Leone, M.2    Vitrano, E.3    Cordone, L.4
  • 15
    • 0018794360 scopus 로고
    • Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes
    • Desbois A, Lutz M, Banarjee R (1979) Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes. Biochemistry 18:1510-1518
    • (1979) Biochemistry , vol.18 , pp. 1510-1518
    • Desbois, A.1    Lutz, M.2    Banarjee, R.3
  • 17
    • 0026700192 scopus 로고
    • Vibrational coupling, spectral broadening mechanisms and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape
    • Di Pace A, Cupane A, Leone M, Vitrano E, Cordone L (1992) Vibrational coupling, spectral broadening mechanisms and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape. Biophys J 63:475-484
    • (1992) Biophys J , vol.63 , pp. 475-484
    • Di Pace, A.1    Cupane, A.2    Leone, M.3    Vitrano, E.4    Cordone, L.5
  • 18
    • 0019761126 scopus 로고
    • Polarized absorption and linear dichroism spectroscopy of hemoglobin
    • Eaton WA, Hofrichter J (1981) Polarized absorption and linear dichroism spectroscopy of hemoglobin. Methods Enzymol 76: 175-261
    • (1981) Methods Enzymol , vol.76 , pp. 175-261
    • Eaton, W.A.1    Hofrichter, J.2
  • 21
    • 0027490333 scopus 로고
    • ε, (His F8) band in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode
    • ε, (His F8) band in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode. Biophys J 65:1470-1485
    • (1993) Biophys J , vol.65 , pp. 1470-1485
    • Gilch, H.1    Schweitzer-Stenner, R.2    Dreybrodt, W.3
  • 24
    • 0023425186 scopus 로고
    • Dynamic properties of oxy- and carbonmonoxyhemoglobin probed by optical spectroscopy in the temperature range 300-20 K
    • Leone M, Cupane A, Vitrano E, Cordone L (1987) Dynamic properties of oxy- and carbonmonoxyhemoglobin probed by optical spectroscopy in the temperature range 300-20 K. Biopolymers 26:1769-1779
    • (1987) Biopolymers , vol.26 , pp. 1769-1779
    • Leone, M.1    Cupane, A.2    Vitrano, E.3    Cordone, L.4
  • 26
    • 0028575357 scopus 로고
    • Thermal broadening of the Soret band in heme complexes and in heme-proteins: Role of iron dynamics
    • Leone M, Cupane A, Cordone L (1994) Thermal broadening of the Soret band in heme complexes and in heme-proteins: role of iron dynamics. Eur Biophys J 23:349-352
    • (1994) Eur Biophys J , vol.23 , pp. 349-352
    • Leone, M.1    Cupane, A.2    Cordone, L.3
  • 27
    • 0011079003 scopus 로고
    • Consistent porphyrin force field. 1. Normal-mode analysis for nickel porphine and nickel tetraphenylporphine from resonance Raman and infrared spectra and isotope shifts
    • Li X-Y, Czernuszewicz RS, Kincaid JR, Su YO, Spiro TG (1990) Consistent porphyrin force field. 1. Normal-mode analysis for nickel porphine and nickel tetraphenylporphine from resonance Raman and infrared spectra and isotope shifts. J Phys Chem 94:31-47
    • (1990) J Phys Chem , vol.94 , pp. 31-47
    • Li, X.-Y.1    Czernuszewicz, R.S.2    Kincaid, J.R.3    Su, Y.O.4    Spiro, T.G.5
  • 28
    • 0001607403 scopus 로고
    • Structural and analytical aspects of the electronic spectra of hemeproteins
    • Lever IABP, Gray HB (eds) Addison-Wesley, Reading Mass
    • Machinen MW, Churg AK (1983) Structural and analytical aspects of the electronic spectra of hemeproteins. In: Lever IABP, Gray HB (eds) Iron porphyrins. Addison-Wesley, Reading Mass, pp 141-235
    • (1983) Iron Porphyrins , pp. 141-235
    • Machinen, M.W.1    Churg, A.K.2
  • 29
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of non linear parameters
    • Marquardt DW (1963) An algorithm for least-squares estimation of non linear parameters. J Soc Ind Appl Math 11:431-441
    • (1963) J Soc Ind Appl Math , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 30
    • 0018692560 scopus 로고
    • A structural model for the kinetic behavior of hemoglobin
    • Moffat K, Deatherage JF, Seybert DW (1979) A structural model for the kinetic behavior of hemoglobin. Science 206:1035-1042
    • (1979) Science , vol.206 , pp. 1035-1042
    • Moffat, K.1    Deatherage, J.F.2    Seybert, D.W.3
  • 31
    • 36749109606 scopus 로고
    • Excited state geometry changes from preresonance Raman intensity: Isoprene and hexatriene
    • Myers AB, Mathies RA, Tannor DJ, Heller EJ (1982) Excited state geometry changes from preresonance Raman intensity: isoprene and hexatriene. J Chem Phys 15:3857-3866
    • (1982) J Chem Phys , vol.15 , pp. 3857-3866
    • Myers, A.B.1    Mathies, R.A.2    Tannor, D.J.3    Heller, E.J.4
  • 32
    • 0000777551 scopus 로고
    • Investigations of Spectral broadening Mechanisms in Biomolecules: Cytochrome-C
    • Schomacker KT, Champion PM (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
  • 33
    • 36549097734 scopus 로고
    • Investigations of the stokes and anti-Stokes resonance Raman scattering of cytochome-C
    • Schomacker KT, Bangcharoenpaurpong O, Champion PM (1984) Investigations of the stokes and anti-Stokes resonance Raman scattering of cytochome-C. J Chem Phys 80:4701-4717
    • (1984) J Chem Phys , vol.80 , pp. 4701-4717
    • Schomacker, K.T.1    Bangcharoenpaurpong, O.2    Champion, P.M.3
  • 34
    • 0001514543 scopus 로고
    • Relationship between structural parameters and Raman frequencies for some planar and nonplanar nickel(II) porphyrins
    • Shelnutt JA, Medforth CJ, Berber MD, Barkigia KM, Smith KM (1991) Relationship between structural parameters and Raman frequencies for some planar and nonplanar nickel(II) porphyrins. J Am Chem Soc 113:4077-4087
    • (1991) J Am Chem Soc , vol.113 , pp. 4077-4087
    • Shelnutt, J.A.1    Medforth, C.J.2    Berber, M.D.3    Barkigia, K.M.4    Smith, K.M.5
  • 35
    • 0001884258 scopus 로고
    • The resonance raman spectroscopy of metallo porphyrins and heme proteins
    • Lever ABP, Gray HB (eds) Addison Wesley, Reading, Mass
    • Spiro TG (1983) The resonance raman spectroscopy of metallo porphyrins and heme proteins. In: Lever ABP, Gray HB (eds) Iron porphyrins II. Addison Wesley, Reading, Mass, pp 89-159
    • (1983) Iron Porphyrins II , pp. 89-159
    • Spiro, T.G.1
  • 36
    • 0025718720 scopus 로고
    • Investigations of optical line shapes and kinetic hole burning in myoglobin
    • Srajer V, Champion PM (1991) Investigations of optical line shapes and kinetic hole burning in myoglobin. Biochemistry 30:7390-7402
    • (1991) Biochemistry , vol.30 , pp. 7390-7402
    • Srajer, V.1    Champion, P.M.2
  • 37
    • 0027524729 scopus 로고
    • The effect of iron displacement out of the porphyrin plane on the resonance Raman spectra of heme proteins and iron porphyrins
    • Stavrov SS (1993) The effect of iron displacement out of the porphyrin plane on the resonance Raman spectra of heme proteins and iron porphyrins. Biophys J 65:1942-1950
    • (1993) Biophys J , vol.65 , pp. 1942-1950
    • Stavrov, S.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.