The active site heme prosthetic group of such species as hemoglobin, the cytochrome P-450s, and the peroxidases is enveloped within a protective hydrophobic environment located adjacent to a binding site for exogeneous compounds. In addition to providing these physical attributes, the protein component also acts as a carrier, transporting the heme to the appropriate cellular environment. We have replaced this proteinoid appendage with a cyclodextrin-based protective sheath to create artificial analogues of heme-containing proteins. Encapsulated within this saccharide-coated barrier, the heme moiety exhibits many of the characteristics typically reserved for its naturally occurring protein-based counterparts.