Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya)
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 fas...
| Main Authors: | , , , , , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
American Crystallographic Association
2015
|
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711634/ |
| id |
pubmed-4711634 |
|---|---|
| recordtype |
oai_dc |
| spelling |
pubmed-47116342016-01-21 Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya) Levantino, M. Lemke, H. T. Schirò, G. Glownia, M. Cupane, A. Cammarata, M. SPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2 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. American Crystallographic Association 2015-05-29 /pmc/articles/PMC4711634/ /pubmed/26798812 http://dx.doi.org/10.1063/1.4921907 Text en © 2015 Author(s). 2329-7778/2015/2(4)/041713/9 All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Levantino, M. Lemke, H. T. Schirò, G. Glownia, M. Cupane, A. Cammarata, M. |
| spellingShingle |
Levantino, M. Lemke, H. T. Schirò, G. Glownia, M. Cupane, A. Cammarata, M. Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya) |
| author_facet |
Levantino, M. Lemke, H. T. Schirò, G. Glownia, M. Cupane, A. Cammarata, M. |
| author_sort |
Levantino, M. |
| title |
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya) |
| title_short |
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya) |
| title_full |
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya) |
| title_fullStr |
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya) |
| title_full_unstemmed |
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya) |
| title_sort |
observing heme doming in myoglobin with femtosecond x-ray absorption spectroscopya) |
| 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. |
| publisher |
American Crystallographic Association |
| publishDate |
2015 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711634/ |
| _version_ |
1613523654716424192 |