Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5374521 | Chemical Physics | 2012 | 8 Pages |
Abstract
⺠We closely examined the temporal behavior of time-resolved resonance Raman spectra of human adult hemoglobin (HbA) and its isolated chains. ⺠The iron-histidine stretching [ν(Fe-His)] frequency showed a downshift of 2 cmâ1 with a time constant of â¼300 ps for HbA and the isolated chains. ⺠The 2-cmâ1ν(Fe-His) downshift in picosecond region seems characteristic to the globin-folded protein with penta-coordinated structure. ⺠It is suggested that the primary metastable form has more disordered orientation of propionates and less strained environment than the deoxy form. ⺠The present study showed that HbA adopts the metastable structure within a few picoseconds and remains little changed in the subnanosecond regime.
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Authors
Yasuhisa Mizutani, Masako Nagai,