| Autor: |
Chung, Taewon, McClain, Taylor P., Alonso-Mori, Roberto, Chollet, Matthieu, Deb, Aniruddha, Garcia-Esparza, Angel T., Huang Ze En, Joel, Lamb, Ryan M., Michocki, Lindsay B., Reinhard, Marco, van Driel, Tim B., Penner-Hahn, James E., Sension, Roseanne J. |
| Zdroj: |
The Journal of Physical Chemistry - Part B; February 2024, Vol. 128 Issue: 6 p1428-1437, 10p |
| Abstrakt: |
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 B12coenzymes. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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