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1992 Fiscal Year Final Research Report Summary

Structural and Functional Analysis of Hemoproteins Under High Pressure by Las Photolysis Measurements

Research Project

Project/Area Number 03453009
Research Category

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

Allocation TypeSingle-year Grants
Research Field 物理化学一般
Research InstitutionKYOTO UNIVERSITY

Principal Investigator

MORISHIMA Isao  Kyoto Univ., Engineering, Professor, 工学部, 教授 (50026093)

Co-Investigator(Kenkyū-buntansha) ISHIMORI Koichiro  Kyoto Univ., Engineering, Instructor, 工学部, 助手 (20192487)
WATANABE Yoshihito  Kyoto Univ., Engineering, Associate Professor, 工学部, 助教授 (10201245)
Project Period (FY) 1991 – 1992
KeywordsMyoglobin / Hemoglobin / High-Pressure Kinetics / Laser Photolysis / Activation Volume / Ligand Binding / Electron Transfer / CO Rebinding
Research Abstract

1. Several site-specific mutants of human myoglobin(Mb) have been prepared in order to examine the influence of highly conserved leucine residues located in the hydrophobic clusters in the heme distal and proximal site on the heme environmental structures and ligand binding properties. Structural and ligand binding characterization of these recombinant proteins were studied by NMR, IR and laser photolysis measurements under different pressures. The leucine 29 mutants exhibited unusual pressure dependence of CO binding rate constant and the resulting pressure dependence of the activation volume implies that pressurization affects the fractional distributions of multi-conformers of Mb so that the fast CO rebinding conformers is increased under pressure.
2. The effects of pressure on the recombination kinetics of CO binding to the isolated alpha and beta chains of human hemoglobin(Hb) were studied. Pressure dependent activation volume change from negative to positive values in the bimolecular CO association reaction was observed for both isolated chains. This finding was attributed to a change in the rate-determining step from the bond formation to the ligand migration process.
3. We have also studied pressure effects on the CO association reaction for cytochrome P-450. It was found that the activation volume is quite sensitive to the presence or absence of the substrate, the molecular structure of the substrate.
4. Finally, we have made a preliminary study on the pressure effect on the intraprotein electron transfer reaction rate.

  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] Masashi Unno: "Pressure Effects on Carbon monoxide Rebinding to the Isolated and Chains of Human Hemoglodin" Biochemistry. 30. 10679-10685 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Shin-ichi Adachi: "Modification of the Distal Imidazole in Myoglobin to N-Tetraxole-Substituted Imidazole and Its Effects on the Heme Environmental Structure and Ligand Binding Properties" Biochemistry. 31. 8613-8618 (1992)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] "Pressure Effects on Carbonmonoxide Rebinding to the alpha and beta Chains of Human Hemoglobin" Biochemistry. 30. 10679-10685 (1991)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] "Modification of the Distal Imidazole in Myoglobin to N-Tetrazole-Substituted Imidazole and Its Effects on the Heme Environmental Structure and Ligand Binding Properties" Biochemistry. 31. 8613-8618 (1992)

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

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Published: 1994-03-24  

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