Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopyaReport as inadecuate

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1 Department of Physics - University of Palermo 2 SLAC National Accelerator Laboratory 3 IBS - UMR 5075 - Institut de biologie structurale 4 IPR - Institut de Physique de Rennes

Abstract : 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

Keywords : Photodissociation Time resolved spectroscopy X-ray absorption near edge structure X-ray absorption spectra X-ray optics

Author: M. Levantino - H. T. Lemke - Giorgio Schirò - M. Glownia - A. Cupane - Marco Cammarata -

Source: https://hal.archives-ouvertes.fr/


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