Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 2664-2669 |
| Number of pages | 6 |
| Journal | Journal of the American Chemical Society |
| Volume | 114 |
| Issue number | 7 |
| DOIs | |
| State | Published - Mar 1 1992 |
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