Journal
STRUCTURAL DYNAMICS-US
Volume 2, Issue 4, Pages -Publisher
AMER INST PHYSICS
DOI: 10.1063/1.4921907
Keywords
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Funding
- PEPS project SASLELX of the CNRS
- University of Rennes 1
- University of Palermo (FFR program)
- University of Palermo (CoRI program)
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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 (similar to 70 fs) relaxation preceding a slower (similar to 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. (C) 2015 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License.
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