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Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c.
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; Solomon, Edward I; Gaffney, Kelly J.
Afiliação
  • Reinhard ME; PULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
  • Mara MW; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Kroll T; Department of Chemistry, Stanford University, Stanford, CA, USA.
  • Lim H; Department of Chemistry, Northwestern University, Evanston, IL, USA.
  • Hadt RG; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Alonso-Mori R; Department of Chemistry, Stanford University, Stanford, CA, USA.
  • Chollet M; Department of Chemistry, Stanford University, Stanford, CA, USA.
  • Glownia JM; Division of Chemistry and Chemical Engineering, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA, USA.
  • Nelson S; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Sokaras D; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Kunnus K; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Driel TBV; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Hartsock RW; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Kjaer KS; PULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
  • Weninger C; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Biasin E; PULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
  • Gee LB; PULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
  • Hodgson KO; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Hedman B; PULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA, USA.
  • Bergmann U; Department of Chemistry, Stanford University, Stanford, CA, USA.
  • Solomon EI; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, USA.
  • Gaffney KJ; Department of Chemistry, Stanford University, Stanford, CA, USA.
Nat Commun ; 12(1): 1086, 2021 02 17.
Article em En | MEDLINE | ID: mdl-33597529
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 (Kß) 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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Compostos Ferrosos / Citocromos c / Ferro / Metais / Metionina Idioma: En Revista: Nat Commun Assunto da revista: BIOLOGIA / CIENCIA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Estados Unidos
Texto completo
Adicionar na Minha BVS
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XML
PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Compostos Ferrosos / Citocromos c / Ferro / Metais / Metionina Idioma: En Revista: Nat Commun Assunto da revista: BIOLOGIA / CIENCIA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Estados Unidos