| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5389761 | Chemical Physics Letters | 2006 | 5 Pages |
Abstract
The role of heme propionates of myoglobin in vibrational energy relaxation was studied by time-resolved resonance Raman spectroscopy. The decay rates of the anti-Stokes intensities of etioheme-substituted myoglobin where the heme lacks the propionates were less than those of wild-type myoglobin, suggesting that the propionates play an important role.
Related Topics
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Physical and Theoretical Chemistry
Authors
Mai Koyama, Saburo Neya, Yasuhisa Mizutani,