Detected as enhanced absorptive or emissive signals in the NMR spectra of the reaction products, CIDNP has been exploited for the last 30 years to characterise transient free radicals and their reaction mechanisms. In certain cases, CIDNP also offers the possibility of large improvements in NMR sensitivity. The principal application of this photo-CIDNP technique, as devised by Kaptein in 1978, has been to proteins in which the aromatic amino acid residues histidine, tryptophan and tyrosine can be polarized using flavins or other aza-aromatics as photosensitisers. The key feature of the method is that only solvent accessible histidine, tryptophan and tyrosine residues can undergo the radical pair reactions that result in nuclear polarization. Photo-CIDNP has thus been used to probe the surface structure of proteins, both in native and partially folded states, and their interactions with molecules that modify the accessibility of the reactive side chains.
Although usually observed in liquids, the photo-CIDNP effect has also been detected in solid state, for example on C and N nuclei in photosynthetic reaction centres, where significant nuclear polarization can accumulate as a result of spin selection processes in the electron transfer reactions.