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Proceedings Paper

Site-selective spectroscopy of myoglobin
Author(s): Takashi Kushida; Atusi Kurita; Yasuo Kanematsu
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Paper Abstract

Site-selective fluorescence spectroscopy and hole-burning spectroscopy have been performed for Zn-substituted myoglobin (ZnMb) in the red spectral region at low temperatures. The site- energy distribution of the chromophore and the fluorescence spectrum of ZnMb in a single site have been obtained from the analysis of laser-induced fluorescence spectra. It has been found that this single-site fluorescence spectrum can be regarded as the homogeneous spectrum. The comparison of the hole spectra between freeze-dried ZnMb powder and ZnMb in glycerol- water mixture shows that the phonon-sideband profiles of these spectra as well as that of the single-site fluorescence spectrum reflect the density of states of vibrational modes of the protein itself. The density of states of low-frequency vibrational modes of ZnMb weighted by the coupling strength between the electrons of the chromophore and the vibrations of the polypeptide chain has been determined from the above-obtained single-site fluorescence spectrum by solving an integral equation numerically.

Paper Details

Date Published: 17 June 1993
PDF: 10 pages
Proc. SPIE 1922, Laser Study of Macroscopic Biosystems, (17 June 1993); doi: 10.1117/12.146181
Show Author Affiliations
Takashi Kushida, Osaka Univ. (Japan)
Atusi Kurita, Osaka Univ. (Japan)
Yasuo Kanematsu, Osaka Univ. (Japan)


Published in SPIE Proceedings Vol. 1922:
Laser Study of Macroscopic Biosystems

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