Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 124, Issue 1, Pages 199-209Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.9b09286
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Funding
- National Science Foundation [NSF-CHE 1464584, NSF-CHE 1836435, NSF-CHE 1565795]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-ACO2-76SF00515]
- NSF-CHE [1428479]
- Direct For Mathematical & Physical Scien [1428479] Funding Source: National Science Foundation
- Division Of Chemistry [1428479] Funding Source: National Science Foundation
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Polarized X-ray absorption near-edge structure (XANES) at the Co K-edge and broadband UV-vis transient absorption are used to monitor the sequential evolution of the excited-state structure of coenzyme B-12 (adenosylcobalamin) over the first picosecond following excitation. The initial state is characterized by sub -100 fs sequential changes around the central cobalt. These are polarized first in the y-direction orthogonal to the transition dipole and 50 fs later in the x-direction along the transition dipole. Expansion of the axial bonds follows on a ca. 200 fs time scale as the molecule moves out of the Franck-Condon active region of the potential energy surface. On the same 200 fs time scale there are electronic changes that result in the loss of stimulated emission and the appearance of a strong absorption at 340 nm. These measurements provide a cobalt-centered movie of the excited molecule as it evolves to the local excited-state minimum.
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