Heme proteins such as cytochrome-c (cyt-c), hemoglobin (Hb), and myoglobin
(Mb) have been successfully encapsulated in sol-gel derived silica matrices
, retaining their spectroscopic properties and chemical function, The therm
al stability of cyt-c was significantly improved by immobilization in a por
ous silica network. Results from optical absorption, resonance Raman, and t
hermal denaturation studies suggest that biomolecules such as cyt-c design
self-specific pores in the silica network according to the size and shape r
equirements of the biomolecule, Hb and Mb, immobilized using the sol-gel pr
ocess, bound ligands similar to the proteins in aqueous buffer, and silica-
encapsulated manganese myoglobin (MnMb) was a viable detector for nitric ox
ide (NO).