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SUMMARY:Structural and allosteric transitions of heme protein sensors prob
 ed from picosecond to second
DTSTART:20191119T140000
DTEND:20191119T150000
DTSTAMP:20261005T163056Z
UID:29e9f8d14e526f5c2cd7b510e03c32bcd6bf1410204039c824770019
CATEGORIES:Conferences - Seminars
DESCRIPTION:Dr. Michel Négrerie\nEcole Polytechnique\, France      
   \nThe human receptor of nitric oxide (NO)\, named soluble guanylate cy
 clase (sGC)\, is a heme protein present in numerous cells and possesses tw
 o functional remote domains: the sensing domain which harbours the heme co
 factor and the catalytic domain which synthesizes cGMP from GTP. The synth
 esis of the cellular messenger cGMP in the catalytic domain is triggered u
 pon NO binding to the heme thanks to a structural allosteric change. Struc
 tural transitions are induced at the heme level by NO binding to and relea
 se from sGC. I will present how time-resolved absorption spectroscopy in t
 he UV-visible range in the broad time range from 1 picosecond to 1 second 
 allowed to probe localized structural events. Structural allosteric transi
 tions of the NO-receptor\, correlated with NO dynamics\, were also detecte
 d. Time-resolved absorption spectroscopy was also used to decipher the mec
 hanism of action of sGC activators which are artificial drugs and act in t
 he absence of NO. The dynamics of heme-bound side-chains\, like methionine
  as the 6th iron ligand in mitochondrial cytochrome c\, could be measured 
 and revealed a conformational change in the protein.\n \n 
LOCATION:CH G1 495 https://plan.epfl.ch/?room==CH%20G1%20495
STATUS:CONFIRMED
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