Abstract
The chemistry of B12 coenzymes is highly sensitive to the nature of their upper axial ligand and can be further tuned by their environment. Methylcobalamin, for example, generates RPs photochemically but undergoes non-radical biochemistry when bound to its dependent enzymes. Owing to the transient nature of the reaction intermediates, it remains a challenge to investigate how their environment controls reactivity. Here, we describe how to use time-resolved electron paramagnetic spectroscopy to directly monitor the generation and evolution of transient radicals that result from the photolysis of a B12 coenzyme. This method produces evolving, spin-polarized spectra that are rich in mechanistic detail.
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