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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Main Authors: 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
Format: Article
Language:English
Published: Nature Portfolio 2021-02-01
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.
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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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