Time-resolved circular dichroism (TRCD) and absorption spectroscopy are used to follow the photolysis reaction of (carbonmonoxy)myoglobin (MbCO). Following the spectral changes associated with the initial loss of CO, a subtle change is observed in the visible absorption spectrum of the Mb product on a time scale of a few hundred nanoseconds. No changes are seen in the CD spectrum of Mb in the visible and near-UV regions subsequent to the loss of CO. The data suggest the existence of an intermediate found after ligand loss from MbCO that is similar in structure to the final Mb product
To clarify the interplay of kinetic hole-burning (KHB), structural relaxation, and ligand migration ...
This year marks the one hundredth anniversary of the first observation of CO photodissociation from ...
Time-resolved infrared spectroscopy with 0.5-ps resolution is used to track the evolution of the CO ...
Time-resolved circular dichroism (TRCD) and absorption spectroscopy are used to follow the photolysi...
International audienceA calculation of the circular dichroism (CD) spectra of carbon monoxy- and deo...
Conformational changes in proteins, which are known to play a paramount role in biophysical processe...
Nanosecond time-resolved magnetic circular dichroism (TRMCD) and time-resolved natural circular dich...
International audienceA thorough absorption and circular dichroism study is performed in carbonmonox...
This work is devoted to the study of photolysis of carbonmonoxy myoglobin (MbCO) followed by time re...
Picosecond absorption spectroscopy is used to examine the position and band shape of the near infrar...
International audienceAn understanding of the first steps of conformational changes in proteins is v...
Picosecond studies of carboxymyoglobin (MbCO) and oxymyoglobin (MbO2) reveal that excitation at 530 ...
ABSTRACT: The temporal shift in the near-IR absorption peak of myoglobin (Mb) following flash photol...
The optical transient absorption spectra at 30 ps and 6.5 ns after photolysis are compared for both ...
We have observed the rate of oxymyoglobin (MbO2) photodissociation at room temperature and carboxymy...
To clarify the interplay of kinetic hole-burning (KHB), structural relaxation, and ligand migration ...
This year marks the one hundredth anniversary of the first observation of CO photodissociation from ...
Time-resolved infrared spectroscopy with 0.5-ps resolution is used to track the evolution of the CO ...
Time-resolved circular dichroism (TRCD) and absorption spectroscopy are used to follow the photolysi...
International audienceA calculation of the circular dichroism (CD) spectra of carbon monoxy- and deo...
Conformational changes in proteins, which are known to play a paramount role in biophysical processe...
Nanosecond time-resolved magnetic circular dichroism (TRMCD) and time-resolved natural circular dich...
International audienceA thorough absorption and circular dichroism study is performed in carbonmonox...
This work is devoted to the study of photolysis of carbonmonoxy myoglobin (MbCO) followed by time re...
Picosecond absorption spectroscopy is used to examine the position and band shape of the near infrar...
International audienceAn understanding of the first steps of conformational changes in proteins is v...
Picosecond studies of carboxymyoglobin (MbCO) and oxymyoglobin (MbO2) reveal that excitation at 530 ...
ABSTRACT: The temporal shift in the near-IR absorption peak of myoglobin (Mb) following flash photol...
The optical transient absorption spectra at 30 ps and 6.5 ns after photolysis are compared for both ...
We have observed the rate of oxymyoglobin (MbO2) photodissociation at room temperature and carboxymy...
To clarify the interplay of kinetic hole-burning (KHB), structural relaxation, and ligand migration ...
This year marks the one hundredth anniversary of the first observation of CO photodissociation from ...
Time-resolved infrared spectroscopy with 0.5-ps resolution is used to track the evolution of the CO ...