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...

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Detalles Bibliográficos
Autores principales: Levantino, M., Lemke, H. T., Schirò, G., Glownia, M., Cupane, A., Cammarata, M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Crystallographic Association 2015
Materias:
SPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711634/
https://www.ncbi.nlm.nih.gov/pubmed/26798812
http://dx.doi.org/10.1063/1.4921907
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author Levantino, M.
Lemke, H. T.
Schirò, G.
Glownia, M.
Cupane, A.
Cammarata, M.
author_facet Levantino, M.
Lemke, H. T.
Schirò, G.
Glownia, M.
Cupane, A.
Cammarata, M.
author_sort Levantino, M.
collection PubMed
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.
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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. Struct Dyn 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.
spellingShingle SPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2
Levantino, M.
Lemke, H. T.
Schirò, G.
Glownia, M.
Cupane, A.
Cammarata, M.
Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya)
title 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_short Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopya)
title_sort observing heme doming in myoglobin with femtosecond x-ray absorption spectroscopya)
topic SPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711634/
https://www.ncbi.nlm.nih.gov/pubmed/26798812
http://dx.doi.org/10.1063/1.4921907
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