Published July 1, 2015 | Version v1
Journal article

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

  • 1. Univ. of Palermo, Palermo (Italy)
  • 2. SLAC National Accelerator Lab., Menlo Park, CA (United States)
  • 3. CNRS - Institut de Biologie Structurale, Grenoble 38044 (France)
  • 4. Univ. of Rennes, Rennes (France)

Description

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

Availability note (English)

Available from: DOI:10.1063/1.4921907 ; DOE Accepted Manuscript full text, or the publishers Best Available Version will be available free of charge after the embargo period from OSTI using http://www.osti.gov/pages/biblio/1190858

Additional details

Publishing Information

Journal Title
Structural Dynamics
Journal Volume
2
Journal Issue
4
Journal Page Range
vp.
ISSN
2329-7778

Optional Information

Funding organization
USDOE Office of Science - SC (United States)
Secondary number(s)
OSTIID--1190858