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Journal articles
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya)
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
Cited literature [53 references]
https://hal-univ-rennes1.archives-ouvertes.fr/hal-01168333
Contributor : Laurent Jonchère <>
Submitted on : Monday, June 29, 2015 - 4:10:21 PM
Last modification on : Tuesday, October 6, 2020 - 4:12:08 PM
Long-term archiving on: : Wednesday, September 16, 2015 - 6:26:44 AM
Contributor : Laurent Jonchère <>
Submitted on : Monday, June 29, 2015 - 4:10:21 PM
Last modification on : Tuesday, October 6, 2020 - 4:12:08 PM
Long-term archiving on: : Wednesday, September 16, 2015 - 6:26:44 AM
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Observing heme doming in myogl...
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