| Literature DB >> 7074195 |
Abstract
We have observed the rate of oxymyoglobin (MbO2) photodissociation at room temperature and carboxymyoglobin (MbCO) photodissociation as a function of temperature (260-10 K) by means of picosecond spectroscopy. The Mb + O2 and Mb + CO photodissociated states have also been characterized. Based on the picosecond experimental data, we postulate that the photodissociation of ligated myoglobin is a nonactivitated process, and the mechanism involves either a small enthalpy barrier or none at all.Mesh:
Substances:
Year: 1982 PMID: 7074195 PMCID: PMC1328808 DOI: 10.1016/S0006-3495(82)84525-6
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033