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Area of Science:

  • Biochemistry
  • Photobiology
  • Structural Biology

Background:

  • Photoreceptor proteins, including those using vitamin B12 derivatives, regulate vital biological processes.
  • The precise molecular mechanisms of B12 photoreception and its distinction from thermal pathways are not fully understood.

Purpose of the Study:

  • To elucidate the photoactivation mechanism of the B12 photoreceptor CarH from nanoseconds to seconds.
  • To understand how light sensing via B12 differs from thermal activation pathways in enzymes.

Main Methods:

  • Time-resolved and temperature-resolved structural and spectroscopic methods.
  • Quantum chemical calculations.
  • Analysis of crystal structures of dark and light-activated states.

Main Results:

  • Detailed description of CarH photoactivation, revealing photocleavage of a cobalt-carbon bond in adenosylcobalamin.
  • Identification of a novel intermediate adduct linking the adenosyl moiety to the cobalt ion.
  • Demonstration that this adduct mediates structural changes and tetramer dissociation, differentiating it from thermal pathways.

Conclusions:

  • The study provides a spatiotemporal understanding of CarH photoactivation, highlighting a unique intermediate adduct.
  • This mechanism bridges photochemical and photobiological timescales, offering insights into B12-dependent photoreceptor function.
  • Findings pave the way for designing novel B12-based photoreceptors for optogenetics.