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Volumn 86, Issue 1 I, 2004, Pages 656-659

Temperature Dependence of the Iron-Histidine Resonance Raman Band of Deoxyheme Proteins: Anharmonic Coupling Versus Distribution over Taxonomic Conformational Substates

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYHEME PROTEIN; HEMOPROTEIN; HISTIDINE DERIVATIVE; HISTIDINE IRON; IRON DERIVATIVE; MYOGLOBIN; UNCLASSIFIED DRUG;

EID: 0347949613     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0006-3495(04)74143-0     Document Type: Letter
Times cited : (3)

References (26)
  • 1
    • 0000040147 scopus 로고
    • Evidence for proximal control of ligand specificity in heme proteins: absorption and Raman studies of cryogenically trapped photoproducts of ligand bound myoglobins
    • A.M. Ahmed B.F. Campbell D. Caruso M.R. Chance M.D. Chavez S.H. Courtney J.M. Friedman I.E.T. Iben M.R. Ondrias M. Yang Evidence for proximal control of ligand specificity in heme proteins: absorption and Raman studies of cryogenically trapped photoproducts of ligand bound myoglobins Chem. Phys. 158 1991 329 351
    • (1991) Chem. Phys. , vol.158 , pp. 329-351
    • Ahmed, A.M.1    Campbell, B.F.2    Caruso, D.3    Chance, M.R.4    Chavez, M.D.5    Courtney, S.H.6    Friedman, J.M.7    Iben, I.E.T.8    Ondrias, M.R.9    Yang, M.10
  • 3
    • 0141852762 scopus 로고
    • Vibronic effects in geometry and stereochemistry of metalloporphyrins and hemoproteins
    • I.B. Bersuker S.S. Stavrov Vibronic effects in geometry and stereochemistry of metalloporphyrins and hemoproteins Chem. Phys. 54 1981 331 340
    • (1981) Chem. Phys. , vol.54 , pp. 331-340
    • Bersuker, I.B.1    Stavrov, S.S.2
  • 4
    • 0002611739 scopus 로고
    • Structure and properties of metalloporphyrins and hemoproteins - the vibronic approach
    • I.B. Bersuker S.S. Stavrov Structure and properties of metalloporphyrins and hemoproteins - the vibronic approach Coord. Chem. Rev. 88 1988 1 68
    • (1988) Coord. Chem. Rev. , vol.88 , pp. 1-68
    • Bersuker, I.B.1    Stavrov, S.S.2
  • 5
    • 18844466828 scopus 로고
    • Pseudo Jahn-Teller effect as a cause of the iron atom displacement from the heme group plane and possible source of trigger mechanism of conformational changes during oxygenation of hemoglobin
    • I.B. Bersuker S.S. Stavrov B.G. Vekhter Pseudo Jahn-Teller effect as a cause of the iron atom displacement from the heme group plane and possible source of trigger mechanism of conformational changes during oxygenation of hemoglobin Biofizika. 24 1979 413 418
    • (1979) Biofizika. , vol.24 , pp. 413-418
    • Bersuker, I.B.1    Stavrov, S.S.2    Vekhter, B.G.3
  • 6
    • 0032728865 scopus 로고    scopus 로고
    • Iron-histidine resonance Raman band of deoxyheme proteins: effects of anharmonic coupling and glass-liquid phase transition
    • A. Bitler S.S. Stavrov Iron-histidine resonance Raman band of deoxyheme proteins: effects of anharmonic coupling and glass-liquid phase transition Biophys. J. 77 1999 2764 2776
    • (1999) Biophys. J. , vol.77 , pp. 2764-2776
    • Bitler, A.1    Stavrov, S.S.2
  • 7
    • 26344449151 scopus 로고
    • Stereochemical aspects of axial ligation in ferrous iron-porphyrins probed by resonance Raman spectroscopy
    • N.K. Chaudhury G.S.S. Saini L. Verma Stereochemical aspects of axial ligation in ferrous iron-porphyrins probed by resonance Raman spectroscopy Spectrochim. Acta 48A 1992 1589 1599
    • (1992) Spectrochim. Acta , vol.48A , pp. 1589-1599
    • Chaudhury, N.K.1    Saini, G.S.S.2    Verma, L.3
  • 8
    • 0030771840 scopus 로고    scopus 로고
    • Vibrational frequency shifts as a probe of hydrogen bonds: thermal expansion and glass transition of myoglobin in mixed solvents
    • F. Demmel W. Doster W. Petry A. Schulte Vibrational frequency shifts as a probe of hydrogen bonds: thermal expansion and glass transition of myoglobin in mixed solvents Eur. Biophys. J. Biophys. Lett. 26 1997 327 335
    • (1997) Eur. Biophys. J. Biophys. Lett. , vol.26 , pp. 327-335
    • Demmel, F.1    Doster, W.2    Petry, W.3    Schulte, A.4
  • 9
    • 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
    • S. Franzen K. Fritsch S.H. Brewer 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 2002 11641 11646
    • (2002) J. Phys. Chem. B. , vol.106 , pp. 11641-11646
    • Franzen, S.1    Fritsch, K.2    Brewer, S.H.3
  • 10
    • 0011139178 scopus 로고
    • Relaxation and disorders in proteins
    • H. Frauenfelder G.U. Nienhaus R.D. Young Relaxation and disorders in proteins R. Richert A. Blumen Disorder Effects on Relaxational Processes 1994 Springer-Verlag Berlin 592 614
    • (1994) , pp. 592-614
    • Frauenfelder, H.1    Nienhaus, G.U.2    Young, R.D.3
  • 11
    • 0028997570 scopus 로고
    • Thermal fluctuations between conformational substates of the Fe2+-Nɛ(HisF8) linkage in deoxymyoglobin probed by the Raman active Fe-Nɛ(HisF8) stretching vibration
    • F8) stretching vibration Biophys. J. 69 1995 214 227
    • (1995) Biophys. J. , vol.69 , pp. 214-227
    • Gilch, H.1    Dreybrodt, W.2    Schweitzer-Stenner, R.3
  • 12
    • 0027490333 scopus 로고
    • Structural heterogeneity of the Fe2+-Nɛ(HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman active iron histidine stretching mode
    • F8) bond in various hemoglobin and myoglobin derivatives probed by the Raman active iron histidine stretching mode Biophys. J. 65 1993 1470 1485
    • (1993) Biophys. J. , vol.65 , pp. 1470-1485
    • Gilch, H.1    Schweitzer-Stenner, R.2    Dreybrodt, W.3
  • 13
    • 0001751094 scopus 로고    scopus 로고
    • Conformational substates of the Fe2+-Nɛ(HisF8) linkage in deoxymyoglobin and hemoglobin probed in parallel by the Raman band of the Fe-His stretching vibration and the near infrared absorption band III
    • F8) linkage in deoxymyoglobin and hemoglobin probed in parallel by the Raman band of the Fe-His stretching vibration and the near infrared absorption band III Int. J. Quantum Chem. 59 1996 301 313
    • (1996) Int. J. Quantum Chem. , vol.59 , pp. 301-313
    • Gilch, H.1    Schweitzer-Stenner, R.2    Dreybrodt, W.3    Leone, M.4    Cupane, A.5    Cordone, L.6
  • 14
    • 0036358696 scopus 로고    scopus 로고
    • Observation of an isotope-sensitive low-frequency Raman band specific to metmyoglobin
    • S. Hirota Y. Mizoguchi O. Yamauchi T. Kitagawa Observation of an isotope-sensitive low-frequency Raman band specific to metmyoglobin J. Biol. Inorg. Chem. 7 2002 217 221
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 217-221
    • Hirota, S.1    Mizoguchi, Y.2    Yamauchi, O.3    Kitagawa, T.4
  • 15
    • 0035201709 scopus 로고    scopus 로고
    • Influence of static and dynamic disorder on the visible and infrared absorption spectra of carbonmonoxy horseradish peroxidase
    • A.D. Kaposi J.M. Vanderkooi W.W. Wright J. Fidy S.S. Stavrov Influence of static and dynamic disorder on the visible and infrared absorption spectra of carbonmonoxy horseradish peroxidase Biophys. J. 81 2001 3472 3482
    • (2001) Biophys. J. , vol.81 , pp. 3472-3482
    • Kaposi, A.D.1    Vanderkooi, J.M.2    Wright, W.W.3    Fidy, J.4    Stavrov, S.S.5
  • 16
    • 0002052550 scopus 로고
    • The heme protein structure and the iron histidine stretching mode
    • T. Kitagawa The heme protein structure and the iron histidine stretching mode T.G. Spiro Biological Application of Raman Spectroscopy 1988 Wiley & Sons New York 97 131
    • (1988) , pp. 97-131
    • Kitagawa, T.1
  • 17
    • 0043013395 scopus 로고    scopus 로고
    • Simple method for isolation of a wide band from a complicated vibrational spectrum
    • M. Korostishevsky S.S. Stavrov Simple method for isolation of a wide band from a complicated vibrational spectrum Vib. Spectrosc. 32 2003 147 154
    • (2003) Vib. Spectrosc. , vol.32 , pp. 147-154
    • Korostishevsky, M.1    Stavrov, S.S.2
  • 18
    • 0020630775 scopus 로고
    • Resonance Raman spectra of photodissociated carbonmonoxy hemoglobin and deoxy hemoglobin at 10K
    • M.R. Ondrias D.L. Rousseau S.R. Simon Resonance Raman spectra of photodissociated carbonmonoxy hemoglobin and deoxy hemoglobin at 10 K J. Biol. Chem. 258 1983 5638 5642
    • (1983) J. Biol. Chem. , vol.258 , pp. 5638-5642
    • Ondrias, M.R.1    Rousseau, D.L.2    Simon, S.R.3
  • 20
    • 0001548481 scopus 로고
    • Anharmonic coupling of soft modes and its influence on the shape of the iron-histidine resonance Raman band of heme-proteins
    • Y.B. Rosenfeld S.S. Stavrov Anharmonic coupling of soft modes and its influence on the shape of the iron-histidine resonance Raman band of heme-proteins Chem. Phys. Lett. 229 1994 457 464
    • (1994) Chem. Phys. Lett. , vol.229 , pp. 457-464
    • Rosenfeld, Y.B.1    Stavrov, S.S.2
  • 21
    • 0001257259 scopus 로고
    • Transient and cryogenic studies of photodissociated hemoglobin and myoglobin
    • D.L. Rousseau J.M. Friedman Transient and cryogenic studies of photodissociated hemoglobin and myoglobin T.G. Spiro Biological Application of Raman Spectroscopy 1988 Wiley & Sons New York 133 215
    • (1988) , pp. 133-215
    • Rousseau, D.L.1    Friedman, J.M.2
  • 22
    • 0023025916 scopus 로고
    • Cryogenic stabilization of myoglobin photoproducts
    • M. Sassaroli S. Dasgupta D.L. Rousseau Cryogenic stabilization of myoglobin photoproducts J. Biol. Chem. 261 1986 13704 13713
    • (1986) J. Biol. Chem. , vol.261 , pp. 13704-13713
    • Sassaroli, M.1    Dasgupta, S.2    Rousseau, D.L.3
  • 23
    • 0034874784 scopus 로고    scopus 로고
    • The Fe2+-HisF8 Raman band shape of deoxymyoglobin reveals taxonomic conformational substates of the proximal linkage
    • F8 Raman band shape of deoxymyoglobin reveals taxonomic conformational substates of the proximal linkage Biophys. J. 81 2001 1624 1631
    • (2001) Biophys. J. , vol.81 , pp. 1624-1631
    • Schott, J.1    Dreybrodt, W.2    Schweitzer-Stenner, R.3
  • 24
    • 0027524729 scopus 로고
    • The effect of iron displacement out of the porphyrin plane on the resonance Raman-spectra of heme-proteins and iron porphyrins
    • S.S. Stavrov The effect of iron displacement out of the porphyrin plane on the resonance Raman-spectra of heme-proteins and iron porphyrins Biophys. J. 65 1993 1942 1950
    • (1993) Biophys. J. , vol.65 , pp. 1942-1950
    • Stavrov, S.S.1
  • 25
    • 0035450575 scopus 로고    scopus 로고
    • Optical absorption band III of deoxyheme proteins as a probe of their structure and dynamics
    • S.S. Stavrov Optical absorption band III of deoxyheme proteins as a probe of their structure and dynamics Chem. Phys. 271 2001 145 154
    • (2001) Chem. Phys. , vol.271 , pp. 145-154
    • Stavrov, S.S.1
  • 26
    • 85120209440 scopus 로고
    • Dependence of the iron-histidine frequency of deoxy heme proteins on the structure of its active center: quantum chemical study
    • S.S. Stavrov B. Kushkuley Dependence of the iron-histidine frequency of deoxy heme proteins on the structure of its active center: quantum chemical study T. Theophanides J. Anastassoupoulou N. Fotopoulos Fifth International Conference on the Spectroscopy of Biological Molecules 1993 Dordrecht, Kluwer Academic Publishers Norwell, MA 305 306
    • (1993) , pp. 305-306
    • Stavrov, S.S.1    Kushkuley, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.