Title of article :
Role of heme propionates of myoglobin in vibrational energy relaxation
Author/Authors :
Koyama، نويسنده , , Mai and Neya، نويسنده , , Saburo and Mizutani، نويسنده , , Yasuhisa، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2006
Pages :
5
From page :
404
To page :
408
Abstract :
The role of heme propionates of myoglobin in vibrational energy relaxation was studied by time-resolved resonance Raman spectroscopy. Time-resolved anti-Stokes spectra were measured to monitor the vibrational energy relaxation of the heme. The decay rates of the band intensities were compared between wild-type myoglobin and etioheme-substituted myoglobin where the heme lacks hydrogen-bonding side chains. The decay rates of the anti-Stokes intensities of the latter were less than those of the former, providing strong support for a theoretical proposal that the propionates and their coupling to solvent bath play an important role in the dissipation of excess energy of the excited heme in solvated wild-type myoglobin.
Journal title :
Chemical Physics Letters
Serial Year :
2006
Journal title :
Chemical Physics Letters
Record number :
1920525
Link To Document :
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