Time-resolved circular dichroism in carbonmonoxy-myoglobin: the central role of the proximal histidine.
A calculation of the circular dichroism (CD) spectra of carbonmonoxy- and deoxy-myoglobin is carried out in relation to a time-resolved CD experiment. This calculation allows us to assign a dominant role to the proximal histidine in the definition of the electronic normal modes and to interpret the transient CD structure observed in a strain of the proximal histidine. This strain builds up in 10 ps and relaxes in 50 ps as the protein evolves towards its deoxy form.
Laboratoire d'Optique et Biosciences, CNRS-INSERM, Ecole Polytechnique, 91128 Palaiseau cedex, France.
Thibault
T
Dartigalongue
François
F
Hache
D002942:Circular Dichroism / Q000379:methods*; D006639:Histidine / Q000737:chemistry*; D009211:Myoglobin / Q000032:analysis* / Q000737:chemistry* / Q000235:genetics; D013056:Spectrophotometry, Ultraviolet; D013997:Time Factors; D014961:X-Ray Diffraction
D009211:Myoglobin; D006639:Histidine