Co-rebinding in myoglobin as seen by time-resolved X-ray absorption spectroscopy

Natali, Francesca; Schmithüsen, Frank
March 2001
European Biophysics Journal;2001, Vol. 30 Issue 1, p63
Academic Journal
Abstract The dynamics of selected conformational coordinates, key roles in the understanding of the CO-rebinding process, are investigated in horse heart carbonmonoxy myoglobin (MbCO) through time-resolved X-ray absorption spectroscopy. We present here the results obtained at 90 K in the second time scale. The approach of the CO molecule towards the Fe atom in the active site pocket is speculated to act as a natural precursor to the Fe displacement with the consequent undoming of the protein porphyrin plane. The arrangement of the Fe-C-O bonding angle geometry follows and the final MbCO active site configuration is completely reached within 1 min.


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