Structural Evolution of Photoexcited Methylcobalamin toward a CarH-like Metastable State: Evidence from Time-Resolved X-ray Absorption and X-ray Emission

Key Points

Photoexcited methylcobalamin undergoes structural evolution toward a CarH-like metastable state, revealing light-driven conformational shifts.
Time-resolved x-ray absorption and x-ray emission spectroscopy track the structural evolution and electronic properties of the photoexcited complex.
Spectroscopic findings highlight how methylcobalamin mimics the protein photoreceptor CarH, supporting models of cobalamin-based light sensing.

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Spectroscopic analysis demonstrates structural evolution in photoexcited methylcobalamin, suggesting formation of a CarH-like metastable state.

CarH is a protein photoreceptor that uses a form of B

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Sension et al. (2024) studied this question.

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