TY - JOUR
T1 - Energy transfer and relaxation mechanisms in Cytochrome c
AU - Consani, C.
AU - Bräm, O.
AU - Van Mourik, F.
AU - Cannizzo, A.
AU - Chergui, M.
PY - 2012
Y1 - 2012
N2 - Using broadband UV–vis femtosecond transient absorption and fluorescence up-conversion, we investigate the interaction between the haem moiety of ferric and ferrous Horse heart Cytochrome c and its single Tryptophan (Trp) residue and the energy dissipation mechanisms upon excitation at various wavelengths in the visible and the UV. Varying the amount of energy deposited in the haem does not affect the relaxation and cooling processes. Differences are observed between the cooling time-scales of the two redox states, which are attributed to different haem–protein couplings. While energy transfer from the Trp to the haem is observed in the decay of Trp and the response of the haem, excitation of the latter does not induce a clear response of the former. This suggests that for Cytochrome c, Trp is not a good marker of the protein response, probably due to its orientation with respect to the haem plane.
AB - Using broadband UV–vis femtosecond transient absorption and fluorescence up-conversion, we investigate the interaction between the haem moiety of ferric and ferrous Horse heart Cytochrome c and its single Tryptophan (Trp) residue and the energy dissipation mechanisms upon excitation at various wavelengths in the visible and the UV. Varying the amount of energy deposited in the haem does not affect the relaxation and cooling processes. Differences are observed between the cooling time-scales of the two redox states, which are attributed to different haem–protein couplings. While energy transfer from the Trp to the haem is observed in the decay of Trp and the response of the haem, excitation of the latter does not induce a clear response of the former. This suggests that for Cytochrome c, Trp is not a good marker of the protein response, probably due to its orientation with respect to the haem plane.
UR - http://www.scopus.com/inward/record.url?eid=2-s2.0-84859540190&partnerID=MN8TOARS
U2 - 10.1016/j.chemphys.2011.09.002
DO - 10.1016/j.chemphys.2011.09.002
M3 - Article
SN - 0301-0104
VL - 396
SP - 108
EP - 115
JO - Chemical Physics
JF - Chemical Physics
ER -