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1994 Fiscal Year Final Research Report Summary

Relationship between structural changes of protein and function of abnormal hemoglobin.

Research Project

Project/Area Number 05670116
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field General medical chemistry
Research InstitutionKanazawa University

Principal Investigator

NAGAI Masako  Kanazawa University, School of Allied Medical Professions, Professor, 医療技術短期大学, 教授 (60019578)

Project Period (FY) 1993 – 1994
KeywordsHemoglobin / Ultraviolet Resonance Raman / Circular Dichroism / Protein Structure / Function of Hemoglobin / Aromatic Amino Acids
Research Abstract

X-ray crystallographic studies have shown that the deoxy and liganded forms of hemoglobin (Hb) poseesee two distinct quaternary structures named T-and R-states, respectively. Cooperative oxygenation to Hb has been explained in terms of a reversible transition between the two quaternary structures upon partial ligation to the four hemes. Environmental changes of tyrosine (Tyr) and tryptophan (Trp) residues of Hb upon its T-to-R transition of quaternary structure was ivestigated with ultraviolet resonance Raman (UVRR) spectroscopy and circular dichroism (CD) . To characterize the spectral change of Trp beta37 at alpha_1beta_2 interface due to the quaternary structure transition, the UVRR spectra of Hb A were compared with the corresponding spectra of Hb Hirose in which Trp beta37 is replaced by serine (Ser) . Difference spectrum between deoxyHb A and deoxyHb Hirose gave rise to only Trp RR bands, which were reasonably ascribed to Trp beta37 in deoxyHb A.Comparison of the Hb A-Hb Hirose difference spectra in the oxy and deoxy states revealed that the oxygenation-induced changes of Trp RR bands arose mostly from Trp beta37 and the remaining minor part from Trp beta15, demonstrating that Trp beta37 plays a pivotal role in the quaternary structural change in Hb A.

  • Research Products

    (12 results)

All Other

All Publications (12 results)

  • [Publications] M.Nagai,S.Kaminaka,Y.Ohba,Y.Nagai,Y.Mizutani,T.Kitagawa: "Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using a tryptophan β37 mutant." Journal of Bilogical Chemistry. 270. 1636-1642 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] A.Dong,M.Nagai,Y.Yoneyama,W.S.Caughey: "Determination of the amounts and oxidation states of Hemoglobins M Boston and M Saskatoon in single erythrocytes by infrared spectroscopy." Journal of Biological Chemistry. 269. 25365-25368 (1994)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] S.Hirota,T.Ogura,K.Shinzawa-Itoh,S.Yoshikawa,M.Nagai,T.Kitagawa: "Vibrational assignments of the FeCO unit of CO-bound heme proteins revisited:Observation of a new CO-isotopesensitive Raman hand assignable to FeCO bonding fundamental." Journal of Physical Chemistry. 98. 6652-6660 (1994)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] M.Nagai,T.Kitagawa: "Resonance Raman and circular dichroic spectra of Hemoglobin Hirose(β37Trp-Ser)." Journal of Inorganic Biochemistry. 51. 126- (1993)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] T.Kitagawa,Y.Sakan,M.Nagai,T.Ogura,F.A.Fraunfelter,T.Kitagawa: "Time-resolved resonance Raman studies of recombination intermediates of CO-photodissociated myoglobin,hemoglobin and its E7 mutants." Journal of Inorganic Biochemistry. 51. 217- (1993)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] T.Lian,B.Locke,T.Kitagawa,M.Nagai,R.M.Hochstrasser: "Determination of Fe-CO geometry in the subunits of Hemoglobin M Boston using femtosecond infrared spectroscopy." Biochemistry. 32. 5809-5814 (1993)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] M.Nagai, S.Kaminaka, Y.Ohba, Y.Nagai, Y.Mizutani, T.Kitagawa: "Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using tryptophan beta37 mutant" J.Biol.Chem.270 (4). 1636-1642 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] A.Dong, M.Nagai, Y.Yoneyama, W.S.Caughey: "Determination of the amounts and oxidation states of Hemoglobins M Boston and M Saskatoon in single erythrocytes by infrared microspectroscopy" J.Biol.Chem.269 (41). 25365-26368 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] S.Hirota, T.Ogura, K.Shinzawa-itoh, S.Yoshikawa, M.Nagai, T.Kitagawa: "Vibrational assignments of the FeCO unit of CO-bound heme proteins revisited : Observation of a new CO-isotope-sensitive Raman band assignable to the FeCO bending fundamental" J.Phys.Chem.98 (26). 6652-6660 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] M.Nagai, T.Kitagawa: "Resonance Raman and circular dichroic spectra of Hemoglobin Hirose (Trp beta37->Ser)" J.lnorg.Biochem.51 (1&2). 126 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] T.Kitagawa, Y.Sakan, M.Nagai, M.Ikeda-Saito: "Time-resolved resonance Raman studies of recombination intermediates of CO-dissociated myoglobin, hemoglobins and its E7 mutants" J.lnorg.Biochem.51 (1&2). 217 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] T.Lian, B.Locke, T.Kitagawa, M.Nagai, R.M.Hochstrasser: "Determination of Fe-CO geometry in the subunits of carbon monoxy Hb M Boston using femtosecond infrared spectroscopy" Biochemistry. 32 (22). 5809-5814 (1993)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1996-04-15  

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