6533b862fe1ef96bd12c6e5c
RESEARCH PRODUCT
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy.
Matteo LevantinoAntonio CupaneM. GlowniaMarco CammarataHenrik T. LemkeGiorgio Schiròsubject
PhotodissociationAbsorption spectroscopyTime resolved spectroscopyInvited ArticlesPhotochemistrySPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2chemistry.chemical_compoundX-ray absorption spectralcsh:QD901-999X-ray absorption near edge structureSpectroscopyInstrumentationHemeSpectroscopy[PHYS]Physics [physics]RadiationX-ray optics[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryPhotodissociationRelaxation (NMR)ChromophoreCondensed Matter PhysicsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)MyoglobinBiofisica Dinamica delle proteine Spettroscopia risolta in tempo X-ray free-electron laser Assorbimento di raggi Xlcsh:CrystallographyTime-resolved spectroscopydescription
International audience; We report time-resolved X-ray absorption measurements after photolysis of carbonmonoxy myoglobin performed at the LCLS X-ray free electron laser with nearly 100 fs (FWHM) time resolution. Data at the Fe K-edge reveal that the photoinduced structural changes at the heme occur in two steps, with a faster (∼70 fs) relaxation preceding a slower (∼400 fs) one. We tentatively attribute the first relaxation to a structural rearrangement induced by photolysis involving essentially only the heme chromophore and the second relaxation to a residual Fe motion out of the heme plane that is coupled to the displacement of myoglobin F-helix
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-07-01 | Structural dynamics (Melville, N.Y.) |