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research article

Energy transfer and relaxation mechanisms in Cytochrome c

Consani, Cristina  
•
Braem, Olivier  
•
van Mourik, Frank  
Show more
2012
Chemical Physics

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. (C) 2011 Elsevier B. V. All rights reserved.

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Type
research article
DOI
10.1016/j.chemphys.2011.09.002
Web of Science ID

WOS:000302767400013

Author(s)
Consani, Cristina  
•
Braem, Olivier  
•
van Mourik, Frank  
•
Cannizzo, Andrea  
•
Chergui, Majed  
Date Issued

2012

Publisher

Elsevier

Published in
Chemical Physics
Volume

396

Start page

108

End page

115

Subjects

Cytochrome c

•

Protein dynamics

•

Tryptophan

•

Ultrafast

•

Pump-probe

•

Ultraviolet-visible

•

Resolved Resonance Raman

•

Primary-Protein Response

•

Carbonmonoxy-Myoglobin

•

Heme-Proteins

•

Transient Absorption

•

Molecular-Dynamics

•

Excited-States

•

Spectroscopy

•

Tryptophan

•

Spectra

Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LSU  
Available on Infoscience
May 11, 2012
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/80269
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