0000000000824122
AUTHOR
Michaela Franke
Recombination studies of photodissociated MbCO by Mössbauer spectroscopy at low temperatures
Rebinding of carbonmonoxide to myoglobin after photodissociation has been studied by Mossbauer spectroscopy at 57.6 K and below for up to 9 days. The time dependence is reproduced by a set of exponentials representing a distribution of activation enthalpies. A shift to smaller values of these activation enthalpies and of the preexponential factor compared to optical studies at higher temperatures has been observed as well as pumping into long-living states.
Molecular tunneling and pumping effects in low temperature MBCO recombination
Recombination of carbonmonoxide after photodissociation has been studied by Mossbauer spectroscopy at 4.2K and in the low temperature region, where tunneling effects play an important role in rebinding. We interpret the kinetic results in terms of a radiationless nonadiabatic multiphonon transition, which leads to a uniform description for all temperatures. Prolonged illumination at low temperature results in pumping into long-living states.