Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy

Matteo Levantino, Antonio Cupane, Schirò, Lemke, Glownia, Marco Cammarata

Risultato della ricerca: Articlepeer review

36 Citazioni (Scopus)


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.
Lingua originaleEnglish
Numero di pagine9
RivistaStructural Dynamics
Stato di pubblicazionePublished - 2015

All Science Journal Classification (ASJC) codes

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  • ???subjectarea.asjc.3100.3105???
  • ???subjectarea.asjc.3100.3104???
  • ???subjectarea.asjc.1600.1607???


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