Yet, little is known about how proteins modulate NO binding or are changed by binding. We have found a spectroscopic way to examine the NO ligated to its principal binding site, which is cysteine, in peptides and albumin.
Protein packing determines orientation of NO in the pocket and also NO reactivity.
We more recently found that photoinduced NO dynamics can occur in skin at a rate exceeding the thermolytic rates. We find that photocleavage displaces NO to other amino acid binding sites. We also observe significant geminate recombination after photolysis, along a path that passes first through one peptide geometry and then into a second one.