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2003 Fiscal Year Final Research Report Summary

Time-Resolved Vibrational Spectroscopic Investigation of Ultrafast Protein Dynamics Coupled with Photoreaction

Research Project

Project/Area Number 12045264
Research Category

Grant-in-Aid for Scientific Research on Priority Areas

Allocation TypeSingle-year Grants
Review Section Science and Engineering
Research InstitutionCenter for Integrative Bioscience, Okazaki National Research Institutes

Principal Investigator

KITAGAWA Teizo  Okazaki National Research Institute, Center for Integrative Bioscience, Professor, 総合バイオサイエンスセンター, 教授 (40029955)

Co-Investigator(Kenkyū-buntansha) MIZUTANI Yasuhisa  Kobe University, Research Center for Molecular Photoscience, Associate Professor, 分子フォトサイエンスセンター, 助教授 (60270469)
Project Period (FY) 2000 – 2001
KeywordsTime-Resolved Raman / Myoglobin / Protein Dynamics / Tertiary Structure Change / Photodissociation / Resonance Raman / Ultraviolet Resonance Raman
Research Abstract

In many biological systems a localized small structural change extends spatially to mesoscopic dimensions to achieve a physiological function, and higher-order structural changes of proteins are essential to this process. Myoglobin (Mb) is one of the best molecules for studying such features of proteins, because photodissociation of CO from carbonmonoxyMb (MbCO), a localized reaction, takes place within 50 fs like a step-function with a quantum yield of nearly unity. It is know from x-ray studies that the iron atom moves out of the porphyrin plane by 〜0.3 A and the core-size expands by 0.05A upon deligation of CO. To explore the protein dynamics involved in this process, we have investigated picosecond time-resolved resonance Raman spectra of photodissociated MbCO.
Close inspection of the spectra of deoxyMb following CO photolysis in the 1300-1650 cm^<-1> region revealed that the core-size expansion of porphyrin ring is completed within the instrumental response time (〜2 ps). In contrast, changes in the intensity and frequency of the Fe-His stretching mode (VFe-His) occurred in picoseconds, suggesting appreciable time evolution for the Fe displacement from the porphyrin plane. The same behaviors were observed for the model compound of the heme group without protein matrix. Therefore, this reflects an intrinsic property of heme itself. On the other hand, the frequency of the VFe-His mode changed with a time constant of 〜100 ps. This frequency change was not seen for the model compound without the protein matrix. Therefore, this must be caused by tertiary structural changes of the protein. Temporal changes of the anti-Stokes Raman intensity of the V_4 and V_7 bands demonstrated immediate generation of the vibrationally excited heme upon photolysis and subsequent decay of the vibrationally excited population with the time constants of 1.1±0.6 and 1.9±0.6 ps, respectively.

  • Research Products

    (12 results)

All Other

All Publications (12 results)

  • [Publications] Y.MIZUTANI: "Ultrafast Dynamics of Myoglobin Probed by Time-Resolved Resonance Raman Spectroscopy"Chem.Records. 1. 258 (2001)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] N.HARUTA: "Protein conformation change of myoglobin upon ligand binding probed by ultraviolet resonance Raman spectroscopy"Biochemistry. 40. 6956 (2001)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Y.MIZUTANI: "Ultrafast structural relaxation of myoglobin following photodissociation of carbon monoxide probed by time-resolved resonance Raman spectroscopy"J.Phys.Chem.. 105. 10992 (2001)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] T.TOMITA: "Purification of Bovine Soluble Guanylate Cyclase and ADP-Ribosylation on Its Small Subunit by Bacterial Toxins"J.Biochem. 122. 531 (1997)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] T.TOMITA: "Effects of GTP on Bound Nitric Oxide of Soluble Guanylate Cyclase Revealed by Resonance Raman Spectroscopy"Biochemistry. 36. 10155 (1997)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] T.KITAGAWA: "Formation of Unphotodissociable CO-Heme Adduct in Soluble Guanylate Cyclase"J.Inorg.Chem.. 96. 23 (2003)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Y.MIZUTANI: "Ultrafast Dynamics of Myoglobin Probed by Time-Resolved Resonance Raman Spectroscopy"Chem. Records. 1. 258 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] N.HARUTA: "Protein conformation change of myoglobin upon ligand binding probed by ultraviolet resonance Raman spectroscopy"Biochemistry. 40. 6956 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Y.MIZUTANI: "Ultrafast structural relaxation of myoglobin following photodissociation of carbon monoxide probed by time-resolved resonance Raman spectroscopy"J. Phys. Chem. 105. 10992 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] T.TOMITA: "Purification of Bovine Soluble Guanylate Cyclase and ADP-Ribosylation on Its Small Subunit by Bacterial Toxins"J. Bioche. 122. 531 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] T.TOMITA: "Effects of GTP on Bound Nitric Oxide of Soluble Guanylate Cyclase Revealed by Resonance Raman Spectroscopy"Biochemistry. 36. 10155 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] T.KITAGAWA: "Formation of Unphotodissociable CO-Heme Adduct in Soluble Guanylate Cyclase"J. Inorg. Chem.. 96. 23 (2003)

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

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Published: 2005-04-19  

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