Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c
The dissociation mechanism of the heme axial ligand in heme proteins is not yet fully understood. The authors investigate the photodissociation dynamics of the bond between heme Fe and methionine S in ferrous cytochrome c using femtosecond time-resolved X-ray solution scattering and X-ray emission s...
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Language: | English |
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Nature Portfolio
2021-02-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-021-21423-w |
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author | Marco E. Reinhard Michael W. Mara Thomas Kroll Hyeongtaek Lim Ryan G. Hadt Roberto Alonso-Mori Matthieu Chollet James M. Glownia Silke Nelson Dimosthenis Sokaras Kristjan Kunnus Tim Brandt van Driel Robert W. Hartsock Kasper S. Kjaer Clemens Weninger Elisa Biasin Leland B. Gee Keith O. Hodgson Britt Hedman Uwe Bergmann Edward I. Solomon Kelly J. Gaffney |
author_facet | Marco E. Reinhard Michael W. Mara Thomas Kroll Hyeongtaek Lim Ryan G. Hadt Roberto Alonso-Mori Matthieu Chollet James M. Glownia Silke Nelson Dimosthenis Sokaras Kristjan Kunnus Tim Brandt van Driel Robert W. Hartsock Kasper S. Kjaer Clemens Weninger Elisa Biasin Leland B. Gee Keith O. Hodgson Britt Hedman Uwe Bergmann Edward I. Solomon Kelly J. Gaffney |
author_sort | Marco E. Reinhard |
collection | DOAJ |
description | The dissociation mechanism of the heme axial ligand in heme proteins is not yet fully understood. The authors investigate the photodissociation dynamics of the bond between heme Fe and methionine S in ferrous cytochrome c using femtosecond time-resolved X-ray solution scattering and X-ray emission spectroscopy, simultaneously tracking electronic and nuclear structure changes. |
first_indexed | 2024-12-14T15:38:08Z |
format | Article |
id | doaj.art-b36cfbe98c1e409a802196ff2da67f18 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-14T15:38:08Z |
publishDate | 2021-02-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-b36cfbe98c1e409a802196ff2da67f182022-12-21T22:55:41ZengNature PortfolioNature Communications2041-17232021-02-011211810.1038/s41467-021-21423-wShort-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome cMarco E. Reinhard0Michael W. Mara1Thomas Kroll2Hyeongtaek Lim3Ryan G. Hadt4Roberto Alonso-Mori5Matthieu Chollet6James M. Glownia7Silke Nelson8Dimosthenis Sokaras9Kristjan Kunnus10Tim Brandt van Driel11Robert W. Hartsock12Kasper S. Kjaer13Clemens Weninger14Elisa Biasin15Leland B. Gee16Keith O. Hodgson17Britt Hedman18Uwe Bergmann19Edward I. Solomon20Kelly J. Gaffney21PULSE Institute, SLAC National Accelerator Laboratory, Stanford UniversityDepartment of Chemistry, Stanford UniversityStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford UniversityDepartment of Chemistry, Stanford UniversityDepartment of Chemistry, Stanford UniversityLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford UniversityLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford UniversityLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford UniversityLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford UniversityStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford UniversityPULSE Institute, SLAC National Accelerator Laboratory, Stanford UniversityLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford UniversityPULSE Institute, SLAC National Accelerator Laboratory, Stanford UniversityPULSE Institute, SLAC National Accelerator Laboratory, Stanford UniversityLinac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford UniversityPULSE Institute, SLAC National Accelerator Laboratory, Stanford UniversityDepartment of Chemistry, Stanford UniversityStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford UniversityStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford UniversityPULSE Institute, SLAC National Accelerator Laboratory, Stanford UniversityStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford UniversityPULSE Institute, SLAC National Accelerator Laboratory, Stanford UniversityThe dissociation mechanism of the heme axial ligand in heme proteins is not yet fully understood. The authors investigate the photodissociation dynamics of the bond between heme Fe and methionine S in ferrous cytochrome c using femtosecond time-resolved X-ray solution scattering and X-ray emission spectroscopy, simultaneously tracking electronic and nuclear structure changes.https://doi.org/10.1038/s41467-021-21423-w |
spellingShingle | Marco E. Reinhard Michael W. Mara Thomas Kroll Hyeongtaek Lim Ryan G. Hadt Roberto Alonso-Mori Matthieu Chollet James M. Glownia Silke Nelson Dimosthenis Sokaras Kristjan Kunnus Tim Brandt van Driel Robert W. Hartsock Kasper S. Kjaer Clemens Weninger Elisa Biasin Leland B. Gee Keith O. Hodgson Britt Hedman Uwe Bergmann Edward I. Solomon Kelly J. Gaffney Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c Nature Communications |
title | Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c |
title_full | Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c |
title_fullStr | Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c |
title_full_unstemmed | Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c |
title_short | Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c |
title_sort | short lived metal centered excited state initiates iron methionine photodissociation in ferrous cytochrome c |
url | https://doi.org/10.1038/s41467-021-21423-w |
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