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- Title
Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c.
- Authors
Reinhard, Marco E.; Mara, Michael W.; Kroll, Thomas; Lim, Hyeongtaek; Hadt, Ryan G.; Alonso-Mori, Roberto; Chollet, Matthieu; Glownia, James M.; Nelson, Silke; Sokaras, Dimosthenis; Kunnus, Kristjan; Driel, Tim Brandt van; Hartsock, Robert W.; Kjaer, Kasper S.; Weninger, Clemens; Biasin, Elisa; Gee, Leland B.; Hodgson, Keith O.; Hedman, Britt; Bergmann, Uwe
- Abstract
The dynamics of photodissociation and recombination in heme proteins represent an archetypical photochemical reaction widely used to understand the interplay between chemical dynamics and reaction environment. We report a study of the photodissociation mechanism for the Fe(II)-S bond between the heme iron and methionine sulfur of ferrous cytochrome c. This bond dissociation is an essential step in the conversion of cytochrome c from an electron transfer protein to a peroxidase enzyme. We use ultrafast X-ray solution scattering to follow the dynamics of Fe(II)-S bond dissociation and 1s3p (Kβ) X-ray emission spectroscopy to follow the dynamics of the iron charge and spin multiplicity during bond dissociation. From these measurements, we conclude that the formation of a triplet metal-centered excited state with anti-bonding Fe(II)-S interactions triggers the bond dissociation and precedes the formation of the metastable Fe high-spin quintet state. 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.
- Subjects
X-ray emission spectroscopy; EXCITED states; CYTOCHROME c; HEMOPROTEINS; PHOTODISSOCIATION; X-ray scattering; NUCLEAR structure
- Publication
Nature Communications, 2021, Vol 12, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-021-21423-w