메뉴 건너뛰기




Volumn 117, Issue 41, 2013, Pages 12461-12468

Intersubunit communication via changes in hemoglobin quaternary structures revealed by time-resolved resonance Raman spectroscopy: Direct observation of the perutz mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC CONTROL; DIRECT OBSERVATIONS; QUATERNARY STRUCTURE; REAL-TIME OBSERVATION; RESONANCE RAMAN SPECTRA; TEMPORAL EVOLUTION; TIME RESOLVED RESONANCE RAMAN SPECTROSCOPY; TIME-RESOLVED SPECTRA;

EID: 84886923558     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp407735t     Document Type: Article
Times cited : (21)

References (45)
  • 1
    • 78651189765 scopus 로고
    • On the Nature of Allosteric Transitions: A Plausible Model
    • Monod, J.; Wyman, J.; Changeux, J. P. On the Nature of Allosteric Transitions: A Plausible Model J. Mol. Biol. 1965, 12, 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 2
    • 0013863816 scopus 로고
    • Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits
    • Koshland, D. E.; Némethy, G.; Filmer, D. Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits Biochemistry 1966, 5, 365-385
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Némethy, G.2    Filmer, D.3
  • 3
    • 0015529611 scopus 로고
    • Nature of Haem-Haem Interaction
    • Perutz, M. F. Nature of Haem-Haem Interaction Nature 1972, 237, 495-499
    • (1972) Nature , vol.237 , pp. 495-499
    • Perutz, M.F.1
  • 5
    • 0014958182 scopus 로고
    • Stereochemistry of Cooperative Effects in Haemoglobin
    • Perutz, M. F. Stereochemistry of Cooperative Effects in Haemoglobin Nature 1970, 228, 726-739
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 6
    • 0018361151 scopus 로고
    • Haemoglobin: The Structural Changes Related to Ligand Binding and Its Allosteric Mechanism
    • Baldwin, J.; Chothia, C. Haemoglobin: The Structural Changes Related to Ligand Binding and Its Allosteric Mechanism J. Mol. Biol. 1979, 129, 175-220
    • (1979) J. Mol. Biol. , vol.129 , pp. 175-220
    • Baldwin, J.1    Chothia, C.2
  • 7
    • 84965066819 scopus 로고
    • The Photochemical Formation of a Quickly Reacting Form of Haemoglobin
    • Gibson, Q. H. The Photochemical Formation of a Quickly Reacting Form of Haemoglobin Biochem. J. 1959, 71, 293-303
    • (1959) Biochem. J. , vol.71 , pp. 293-303
    • Gibson, Q.H.1
  • 8
    • 0021486088 scopus 로고
    • Tertiary-Structure Relaxation in Hemoglobin - A Transient Raman-Study
    • Scott, T. W.; Friedman, J. M. Tertiary-Structure Relaxation in Hemoglobin-a Transient Raman-Study J. Am. Chem. Soc. 1984, 106, 5677-5687
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5677-5687
    • Scott, T.W.1    Friedman, J.M.2
  • 9
    • 0028927331 scopus 로고
    • Evidence for Sub-Picosecond Heme Doming in Hemoglobin and Myoglobin: A Time-Resolved Resonance Raman Comparison of Carbonmonoxy and Deoxy Species
    • Franzen, S.; Bohn, B.; Poyart, C.; Martin, J. L. Evidence for Sub-Picosecond Heme Doming in Hemoglobin and Myoglobin: A Time-Resolved Resonance Raman Comparison of Carbonmonoxy and Deoxy Species Biochemistry 1995, 34, 1224-1237
    • (1995) Biochemistry , vol.34 , pp. 1224-1237
    • Franzen, S.1    Bohn, B.2    Poyart, C.3    Martin, J.L.4
  • 10
    • 84857285196 scopus 로고    scopus 로고
    • Protein Dynamics of Isolated Chains of Recombinant Human Hemoglobin Elucidated by Time-Resolved Resonance Raman Spectroscopy
    • Yamada, K.; Ishikawa, H.; Mizutani, Y. Protein Dynamics of Isolated Chains of Recombinant Human Hemoglobin Elucidated by Time-Resolved Resonance Raman Spectroscopy J. Phys. Chem. B 2012, 116, 1992-1998
    • (2012) J. Phys. Chem. B , vol.116 , pp. 1992-1998
    • Yamada, K.1    Ishikawa, H.2    Mizutani, Y.3
  • 11
    • 0027993426 scopus 로고
    • Nanosecond Dynamics of the R→T Transition in Hemoglobin: Ultraviolet Raman Studies
    • Rodgers, K. R.; Spiro, T. G. Nanosecond Dynamics of the R→T Transition in Hemoglobin: Ultraviolet Raman Studies Science 1994, 265, 1697-1699
    • (1994) Science , vol.265 , pp. 1697-1699
    • Rodgers, K.R.1    Spiro, T.G.2
  • 12
    • 0028799067 scopus 로고
    • Hemoglobin Allostery: Resonance Raman Spectroscopy of Kinetic Intermediates
    • Jayaraman, V.; Rodgers, K. R.; Mukerji, I.; Spiro, T. G. Hemoglobin Allostery: Resonance Raman Spectroscopy of Kinetic Intermediates Science 1995, 269, 1843-1848
    • (1995) Science , vol.269 , pp. 1843-1848
    • Jayaraman, V.1    Rodgers, K.R.2    Mukerji, I.3    Spiro, T.G.4
  • 13
    • 3042521090 scopus 로고    scopus 로고
    • Time-Resolved Absorption and UV Resonance Raman Spectra Reveal Stepwise Formation of T Quaternary Contacts in the Allosteric Pathway of Hemoglobin
    • Balakrishnan, G.; Case, M. A.; Pevsner, A.; Zhao, X.; Tengroth, C.; McLendon, G. L.; Spiro, T. G. Time-Resolved Absorption and UV Resonance Raman Spectra Reveal Stepwise Formation of T Quaternary Contacts in the Allosteric Pathway of Hemoglobin J. Mol. Biol. 2004, 340, 843-856
    • (2004) J. Mol. Biol. , vol.340 , pp. 843-856
    • Balakrishnan, G.1    Case, M.A.2    Pevsner, A.3    Zhao, X.4    Tengroth, C.5    McLendon, G.L.6    Spiro, T.G.7
  • 14
  • 16
    • 17544382025 scopus 로고    scopus 로고
    • Oxygen Equilibrium Properties of Chromium (III)-Iron (II) Hybrid Hemoglobins
    • Unzai, S.; Hori, H.; Miyazaki, G.; Shibayama, N.; Morimoto, H. Oxygen Equilibrium Properties of Chromium (III)-Iron (II) Hybrid Hemoglobins J. Biol. Chem. 1996, 271, 12451-12456
    • (1996) J. Biol. Chem. , vol.271 , pp. 12451-12456
    • Unzai, S.1    Hori, H.2    Miyazaki, G.3    Shibayama, N.4    Morimoto, H.5
  • 17
    • 0021766916 scopus 로고
    • Carbon Monoxide Binding to the Ferrous Chains of [Mn,Fe(II)] Hybrid Hemoglobins: PH Dependence of the Chain Affinity Constants Associated with Specific Hemoglobin Ligation Pathways
    • Blough, N. V.; Hoffman, B. M. Carbon Monoxide Binding to the Ferrous Chains of [Mn,Fe(II)] Hybrid Hemoglobins: pH Dependence of the Chain Affinity Constants Associated with Specific Hemoglobin Ligation Pathways Biochemistry 1984, 23, 2875-2882
    • (1984) Biochemistry , vol.23 , pp. 2875-2882
    • Blough, N.V.1    Hoffman, B.M.2
  • 18
    • 0018855972 scopus 로고
    • Studies on Cobalt Myoglobins and Hemoglobins. XI. The Interaction of Carbon Monoxide and Oxygen with α and β Subunits in Iron-Cobalt Hybrid Hemoglobins
    • Ikeda-Saito, M.; Yonetani, T. Studies on Cobalt Myoglobins and Hemoglobins. XI. The Interaction of Carbon Monoxide and Oxygen with α and β Subunits in Iron-Cobalt Hybrid Hemoglobins J. Mol. Biol. 1980, 138, 845-858
    • (1980) J. Mol. Biol. , vol.138 , pp. 845-858
    • Ikeda-Saito, M.1    Yonetani, T.2
  • 19
    • 0018533206 scopus 로고
    • Effect of Removal of a Salt-Bridge on the Oxygen Binding Properties and the Electronic Structure of Heme in Cobalt-Iron Hybrid Hemoglobin
    • Tsubaki, M.; Nagai, K. Effect of Removal of a Salt-Bridge on the Oxygen Binding Properties and the Electronic Structure of Heme in Cobalt-Iron Hybrid Hemoglobin J. Biochem. 1979, 86, 1029-1035
    • (1979) J. Biochem. , vol.86 , pp. 1029-1035
    • Tsubaki, M.1    Nagai, K.2
  • 20
    • 0022966804 scopus 로고
    • Oxygen Equilibrium Study and Light Absorption Spectra of Ni(II)-Fe(II) Hybrid Hemoglobins
    • Shibayama, N.; Morimoto, H.; Miyazaki, G. Oxygen Equilibrium Study and Light Absorption Spectra of Ni(II)-Fe(II) Hybrid Hemoglobins J. Mol. Biol. 1986, 192, 323-329
    • (1986) J. Mol. Biol. , vol.192 , pp. 323-329
    • Shibayama, N.1    Morimoto, H.2    Miyazaki, G.3
  • 21
    • 0023022798 scopus 로고
    • Properties of Chemically Modified Ni(II)-Fe(II) Hybrid Hemoglobins. Ni(II) Protoporphyrin IX as a Model for a Permanent Deoxy-Heme
    • Shibayama, N.; Morimoto, H.; Kitagawa, T. Properties of Chemically Modified Ni(II)-Fe(II) Hybrid Hemoglobins. Ni(II) Protoporphyrin IX as a Model for a Permanent Deoxy-Heme J. Mol. Biol. 1986, 192, 331-336
    • (1986) J. Mol. Biol. , vol.192 , pp. 331-336
    • Shibayama, N.1    Morimoto, H.2    Kitagawa, T.3
  • 22
    • 0029080296 scopus 로고
    • Oxygen Equilibrium and Electron Paramagnetic Resonance Studies on Copper(II)-Iron(II) Hybrid Hemoglobins at Room Temperature
    • Shibayama, N.; Ikeda-Saito, M.; Hori, H.; Itaroku, K.; Morimoto, H.; Saigo, S. Oxygen Equilibrium and Electron Paramagnetic Resonance Studies on Copper(II)-Iron(II) Hybrid Hemoglobins at Room Temperature FEBS Lett. 1995, 372, 126-130
    • (1995) FEBS Lett. , vol.372 , pp. 126-130
    • Shibayama, N.1    Ikeda-Saito, M.2    Hori, H.3    Itaroku, K.4    Morimoto, H.5    Saigo, S.6
  • 23
    • 0000721403 scopus 로고
    • Characterization of Partially Ligated Hemoglobins - NMR, ENDOR, CD, and Stopped-Flow Studies of Zinc-Containing Hemoglobin Hybrids
    • Simolo, K.; Stucky, G.; Chen, S.; Bailey, M.; Scholes, C.; Mclendon, G. Characterization of Partially Ligated Hemoglobins-NMR, ENDOR, CD, and Stopped-Flow Studies of Zinc-Containing Hemoglobin Hybrids J. Am. Chem. Soc. 1985, 107, 2865-2872
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2865-2872
    • Simolo, K.1    Stucky, G.2    Chen, S.3    Bailey, M.4    Scholes, C.5    McLendon, G.6
  • 24
    • 0020479431 scopus 로고
    • Quaternary Structure Changes in Iron-Cobalt Hybrid Hemoglobins Detected by Resonance Raman Scattering
    • Ondrias, M. R.; Rousseau, D. L.; Kitagawa, T.; Ikeda-Saito, M.; Inubushi, T.; Yonetani, T. Quaternary Structure Changes in Iron-Cobalt Hybrid Hemoglobins Detected by Resonance Raman Scattering J. Biol. Chem. 1982, 257, 8766-8770
    • (1982) J. Biol. Chem. , vol.257 , pp. 8766-8770
    • Ondrias, M.R.1    Rousseau, D.L.2    Kitagawa, T.3    Ikeda-Saito, M.4    Inubushi, T.5    Yonetani, T.6
  • 25
    • 77950548846 scopus 로고    scopus 로고
    • 2 and Acts as a Gate for Ligand Entry in Both Subunits of Adult Human Hemoglobin
    • 2 and Acts as a Gate for Ligand Entry in Both Subunits of Adult Human Hemoglobin J. Biol. Chem. 2010, 285, 8840-8854
    • (2010) J. Biol. Chem. , vol.285 , pp. 8840-8854
    • Birukou, I.1    Schweers, R.L.2    Olson, J.S.3
  • 26
    • 0028245069 scopus 로고
    • Expression of Recombinant Human Hemoglobin in Escherichia Coli
    • Looker, D.; Mathews, A. J.; Neway, J. O.; Stetler, G. L. Expression of Recombinant Human Hemoglobin in Escherichia Coli Methods Enzymol. 1994, 231, 364-374
    • (1994) Methods Enzymol. , vol.231 , pp. 364-374
    • Looker, D.1    Mathews, A.J.2    Neway, J.O.3    Stetler, G.L.4
  • 27
    • 0019763671 scopus 로고
    • Preparation and Properties of Apohemoglobin and Reconstituted Hemoglobins
    • Ascoli, F.; Fanelli, M. R.; Antonini, E. Preparation and Properties of Apohemoglobin and Reconstituted Hemoglobins Methods Enzymol. 1981, 76, 72-87
    • (1981) Methods Enzymol. , vol.76 , pp. 72-87
    • Ascoli, F.1    Fanelli, M.R.2    Antonini, E.3
  • 28
    • 0035829917 scopus 로고    scopus 로고
    • Ultrafast Structural Relaxation of Myoglobin Following Photodissociation of Carbon Monoxide Probed by Time-Resolved Resonance Raman Spectroscopy
    • Mizutani, Y.; Kitagawa, T. Ultrafast Structural Relaxation of Myoglobin Following Photodissociation of Carbon Monoxide Probed by Time-Resolved Resonance Raman Spectroscopy J. Phys. Chem. B 2001, 105, 10992-10999
    • (2001) J. Phys. Chem. B , vol.105 , pp. 10992-10999
    • Mizutani, Y.1    Kitagawa, T.2
  • 29
    • 0018792074 scopus 로고
    • e (His F8) Stretching Band in the Resonance Raman Spectra of Deoxy Myoglobin
    • e (His F8) Stretching Band in the Resonance Raman Spectra of Deoxy Myoglobin FEBS Lett. 1979, 104, 376-378
    • (1979) FEBS Lett. , vol.104 , pp. 376-378
    • Kitagawa, T.1    Nagai, K.2    Tsubaki, M.3
  • 30
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of Protoheme Resonance Raman Spectrum by Heme Labeling in Myoglobin
    • Hu, S. Z.; Smith, K. M.; Spiro, T. G. Assignment of Protoheme Resonance Raman Spectrum by Heme Labeling in Myoglobin J. Am. Chem. Soc. 1996, 118, 12638-12646
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12638-12646
    • Hu, S.Z.1    Smith, K.M.2    Spiro, T.G.3
  • 31
    • 0022494586 scopus 로고
    • Four- and Five-Coordinate Species in Nickel-Reconstituted Hemoglobin and Myoglobin: Raman Identification of the Nickel-Histidine Stretching Mode
    • Shelnutt, J. A.; Alston, K.; Ho, J. Y.; Yu, N. T.; Yamamoto, T.; Rifkind, J. M. Four- and Five-Coordinate Species in Nickel-Reconstituted Hemoglobin and Myoglobin: Raman Identification of the Nickel-Histidine Stretching Mode Biochemistry 1986, 25, 620-627
    • (1986) Biochemistry , vol.25 , pp. 620-627
    • Shelnutt, J.A.1    Alston, K.2    Ho, J.Y.3    Yu, N.T.4    Yamamoto, T.5    Rifkind, J.M.6
  • 32
    • 0035756040 scopus 로고    scopus 로고
    • Ultrafast Dynamics of Myoglobin Probed by Time-Resolved Resonance Raman Spectroscopy
    • Mizutani, Y.; Kitagawa, T. Ultrafast Dynamics of Myoglobin Probed by Time-Resolved Resonance Raman Spectroscopy Chem. Rec. 2001, 1, 258-275
    • (2001) Chem. Rec. , vol.1 , pp. 258-275
    • Mizutani, Y.1    Kitagawa, T.2
  • 33
    • 0033596899 scopus 로고    scopus 로고
    • New Light on Allostery: Dynamic Resonance Raman Spectroscopy of Hemoglobin Kempsey
    • Hu, X.; Rodgers, K. R.; Mukerji, I.; Spiro, T. G. New Light on Allostery: Dynamic Resonance Raman Spectroscopy of Hemoglobin Kempsey Biochemistry 1999, 38, 3462-3467
    • (1999) Biochemistry , vol.38 , pp. 3462-3467
    • Hu, X.1    Rodgers, K.R.2    Mukerji, I.3    Spiro, T.G.4
  • 34
    • 33847085258 scopus 로고
    • Iron-Ligand Stretching Band in the Resonance Raman-Spectra of Ferrous Iron Porphyrin Derivatives - Importance as a Probe Band for Quaternary Structure of Hemoglobin
    • Hori, H.; Kitagawa, T. Iron-Ligand Stretching Band in the Resonance Raman-Spectra of Ferrous Iron Porphyrin Derivatives-Importance as a Probe Band for Quaternary Structure of Hemoglobin J. Am. Chem. Soc. 1980, 102, 3608-3613
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 3608-3613
    • Hori, H.1    Kitagawa, T.2
  • 35
    • 0002052550 scopus 로고
    • The Heme Protein Structure and the Iron Histidine Stretching Mode
    • Spiro, T. G. John Wiley and Sons: New York
    • Kitagawa, T. The Heme Protein Structure and the Iron Histidine Stretching Mode. In Biological Application on Raman Spectroscopy; Spiro, T. G., Ed.; John Wiley and Sons: New York, 1988; Vol. III, pp 97-131.
    • (1988) Biological Application on Raman Spectroscopy , vol.3 , pp. 97-131
    • Kitagawa, T.1
  • 36
    • 0001257259 scopus 로고
    • Transient and Cryogenic Studies of Photodissociated Hemoglobin and Myoglobin
    • Spiro, T. G. John Wiley and Sons: New York
    • Rousseau, D. L.; Friedman, J. M. Transient and Cryogenic Studies of Photodissociated Hemoglobin and Myoglobin. In Biological Application on Raman Spectroscopy; Spiro, T. G., Ed.; John Wiley and Sons: New York, 1988; Vol. III, pp 133-216.
    • (1988) Biological Application on Raman Spectroscopy , vol.3 , pp. 133-216
    • Rousseau, D.L.1    Friedman, J.M.2
  • 38
    • 0021051045 scopus 로고
    • Hemoglobin Tertiary Structural Change on Ligand Binding. Its Role in the Co-Operative Mechanism
    • Gelin, B. R.; Lee, A. W.; Karplus, M. Hemoglobin Tertiary Structural Change on Ligand Binding. Its Role in the Co-Operative Mechanism J. Mol. Biol. 1983, 171, 489-559
    • (1983) J. Mol. Biol. , vol.171 , pp. 489-559
    • Gelin, B.R.1    Lee, A.W.2    Karplus, M.3
  • 39
    • 0001244916 scopus 로고
    • e(His-F8) Stretching Frequencies between Deoxyhemoglobins in the Two Alternative Quaternary Structures
    • e(His-F8) Stretching Frequencies between Deoxyhemoglobins in the Two Alternative Quaternary Structures Proc. Natl. Acad. Sci. U.S.A. 1980, 77, 2033-2037
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 2033-2037
    • Nagai, K.1    Kitagawa, T.2
  • 40
    • 84859524386 scopus 로고    scopus 로고
    • Ultrafast Protein Dynamics of Hemoglobin as Studied by Picosecond Time-Resolved Resonance Raman Spectroscopy
    • Mizutani, Y.; Nagai, M. Ultrafast Protein Dynamics of Hemoglobin as Studied by Picosecond Time-Resolved Resonance Raman Spectroscopy Chem. Phys. 2012, 396, 45-52
    • (2012) Chem. Phys. , vol.396 , pp. 45-52
    • Mizutani, Y.1    Nagai, M.2
  • 41
    • 0034045353 scopus 로고    scopus 로고
    • Resonance Raman Studies of Heme Structural Differences in Subunits of Deoxy Hemoglobin
    • Podstawka, E.; Rajani, C.; Kincaid, J. R.; Proniewicz, L. M. Resonance Raman Studies of Heme Structural Differences in Subunits of Deoxy Hemoglobin Biopolymers 2000, 57, 201-207
    • (2000) Biopolymers , vol.57 , pp. 201-207
    • Podstawka, E.1    Rajani, C.2    Kincaid, J.R.3    Proniewicz, L.M.4
  • 42
    • 0022256268 scopus 로고
    • Nanosecond Optical Spectra of Iron-Cobalt Hybrid Hemoglobins: Geminate Recombination, Conformational Changes, and Intersubunit Communication
    • Hofrichter, J.; Henry, E. R.; Sommer, J. H.; Deutsch, R.; Ikeda-Saito, M.; Yonetani, T.; Eaton, W. A. Nanosecond Optical Spectra of Iron-Cobalt Hybrid Hemoglobins: Geminate Recombination, Conformational Changes, and Intersubunit Communication Biochemistry 1985, 24, 2667-2679
    • (1985) Biochemistry , vol.24 , pp. 2667-2679
    • Hofrichter, J.1    Henry, E.R.2    Sommer, J.H.3    Deutsch, R.4    Ikeda-Saito, M.5    Yonetani, T.6    Eaton, W.A.7
  • 45
    • 33845378088 scopus 로고
    • Correlation between the Iron Histidine Stretching Frequencies and Oxygen-Affinity of Hemoglobins - A Continuous Strain Model
    • Matsukawa, S.; Mawatari, K.; Yoneyama, Y.; Kitagawa, T. Correlation between the Iron Histidine Stretching Frequencies and Oxygen-Affinity of Hemoglobins-a Continuous Strain Model J. Am. Chem. Soc. 1985, 107, 1108-1113
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 1108-1113
    • Matsukawa, S.1    Mawatari, K.2    Yoneyama, Y.3    Kitagawa, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.