Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya) - Université de Rennes Accéder directement au contenu
Article Dans Une Revue Structural Dynamics Année : 2015

Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya)

Résumé

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
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Dates et versions

hal-01168333 , version 1 (29-06-2015)

Identifiants

Citer

M. Levantino, H. T. Lemke, Giorgio Schirò, M. Glownia, A. Cupane, et al.. Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya). Structural Dynamics, 2015, 2 (4), pp.041713. ⟨10.1063/1.4921907⟩. ⟨hal-01168333⟩
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