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Studies on Hemoglobin Cooperativity with the Aid of Resonance Raman Spectroscopy and Fluorescence-Labelled Allosteric Effectors.

Research Project

Project/Area Number 60480134
Research Category

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

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

Principal Investigator

YONEYAMA Yoshimasa  Professor, Kanazawa University School of Medicine., 医学部, 教授 (10019515)

Co-Investigator(Kenkyū-buntansha) MAWATARI Kazuhiro  Lecturer, Kanazawa University School of Allied Medical Professions., 医療技術短期大学部, 講師 (50135050)
MATSUKAWA Shigeru  Lecturer, Kanazawa University School of Medicine., 医学部, 講師 (00092809)
Project Period (FY) 1985 – 1986
Project Status Completed (Fiscal Year 1986)
Budget Amount *help
¥6,100,000 (Direct Cost: ¥6,100,000)
Fiscal Year 1986: ¥2,700,000 (Direct Cost: ¥2,700,000)
Fiscal Year 1985: ¥3,400,000 (Direct Cost: ¥3,400,000)
KeywordsHemoglobin / Oxygen affinity / Cooperativity / Resonance Raman / Iron-Histidine bond / 蛍光ラベル / エフェクター
Research Abstract

The outline of the stereochemical mechanism of the cooperative oxygen binding of hemoglobin (Hb) has been well documented. However, the modulation mechanism of oxygen affinity and the trigger mechanism for the R-T structural transition remain unproven experimentally. To resolve these problems we have been investigated the structural and functional relationships of abnormal Hbs with an amino acid substitution at the <(alpha)_1(beta)_2> contact. The aim of this study is to point out the structural element(s) essential for allosteric oxygen binding by comparing the structural alterations with functional ones of various abnormal Hbs.
Analysis of Oxygen equilibrium curves for normal and abnormal Hbs in terms of the two-state allosteric model suggested that the abnormal allosteric oxygen binding of Hb is due to altered molecular properties of the deoxy-T state. To clarify the molecular basis of this situation, the resonance Raman spectra in the low-frequency region of deoxy Hbs and the binding of fluorescence-labelled allosteric effector (MANT-ATP) to deoxy Hbs were examined.
The high-affinity deoxy Hb gave the Fe-His stretching Raman line at 220-220 <cm^(-1)> similar to that of the isolated chains, while the low-affinity one gave the Raman line at 214-216 <cm^(-1)> . However, deoxy Hbs with intermediate levels of oxygen affinity unexpectedly exhibited the Raman line at intermediate frequencies. Furthermore, this varied frequencies of Fe-His stretching Raman lines for various Hbs was found to correlate well with varied oxygen affinities of deoxy-T state. In contrast, the MANT-ATP binding experiments showed that the stucture of the organic phosphate binding site of abnormal Hbs is almost identical to that of Hb A.
Based on the above results, we concluded that the Fe-His bond presumably comprises an important part of the regulation mechanism for hemoglobin oxygen affinity and quaternary structural changes.

Report

(1 results)
  • 1986 Final Research Report Summary
  • Research Products

    (13 results)

All Other

All Publications (13 results)

  • [Publications] 松川茂: J.Am.Chem.Soc.107. 1108-1113 (1985)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 松川茂: Acta Haematol.Jpn.48. 2002-2014 (1985)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 松川茂: J.Protein Chem.6. 109-119 (1987)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 馬渡一浩: Biomed.Biochim.Acta. 印刷中. (1987)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 馬渡一浩: Biochim.Biophys.Acta. 印刷中. (1987)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 馬渡一浩: Biochim.Biophys.Acta. (1987)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 米山良昌: "血色素の分子生理と分子病理" 共立出版, (1987)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Shigeru MATSUKAWA: "Correlation between the Iron-Histidine Stretching Frequencies and Oxygen Affinity of Hemoglobins. A Continuous Strain Model." J. Am. Chem. Soc.107. 1108-1113. (1985)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Shigeru MATSUKAWA: "Allosteric Mechanism Deduced from the Analysis of the Variation of Structure and Function of Abnormal Hemoglobins." Acta Haematol. Jpn.48. 2002-2014. (1985)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Shigeru MATSUKAWA: "Functional and Structural Analyses on Abnormal Hemoglobins with Impaired Oxygen Binding Properties-- To Elucidate the Allosteric Mechanism of Hemoglobin." J. Protein Chem.6. 109-119. (1987)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Kazuhiro MAWATARI: "Valency Hybrid Hemoglobins with Special Attention to Subunit Organization." Biomed. Biochim. Acta. in press. (1987)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Kazuhiro MAWATARI: "Assessment of <(alpha)_1(beta)_2> Contact Structure of Valency Hybrid Hemoglobins by Ultraviolet Difference Spectra." Biochim. Biophys. Acta. in press. (1987)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Yoshimasa YONEYAMA: Kyoritsu Shuppan Co., Ltd.Molecular Physiology and Pathology of Hemoglobin, (1987)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary

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Published: 1987-03-31   Modified: 2016-04-21  

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