Ultrafast X-ray Absorption Spectroscopy Reveals Excited-State Dynamics of B 12 Coenzymes Controlled by the Axial Base.

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  • Additional Information
    • Source:
      Publisher: American Chemical Society Country of Publication: United States NLM ID: 101157530 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5207 (Electronic) Linking ISSN: 15205207 NLM ISO Abbreviation: J Phys Chem B Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, D.C. : American Chemical Society, c1997-
    • Subject Terms:
      Coenzymes* ; Vitamin B 12*/chemistry; X-Ray Absorption Spectroscopy ; Photolysis
    • Abstract:
      Polarized time-resolved X-ray absorption spectroscopy at the Co K-edge is used to probe the excited-state dynamics and photolysis of base-off methylcobalamin and the excited-state structure of base-off adenosylcobalamin. For both molecules, the final excited-state minimum shows evidence for an expansion of the cavity around the Co ion by ca. 0.04 to 0.05 Å. The 5-coordinate base-off cob(II)alamin that is formed following photodissociation has a structure similar to that of the 5-coordinate base-on cob(II)alamin, with a ring expansion of 0.03 to 0.04 Å and a contraction of the lower axial bond length relative to that in the 6-coordinate ground state. These data provide insights into the role of the lower axial ligand in modulating the reactivity of B 12 coenzymes.
    • Accession Number:
      0 (Coenzymes)
      P6YC3EG204 (Vitamin B 12)
    • Publication Date:
      Date Created: 20240201 Date Completed: 20240216 Latest Revision: 20240216
    • Publication Date:
      20240216
    • Accession Number:
      10.1021/acs.jpcb.3c07779
    • Accession Number:
      38301132