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Accessibility of oxygen with respect to the heme pocket in horseradish peroxidase
2003
Proteins: Structure, Function, and Bioinformatics
Oxygen and other molecules of similar size take part in a variety of protein reactions. Therefore, it is critical to understand how these small molecules penetrate the protein matrix. The protein system studied in this case is horseradish peroxidase (HRP). We have converted the native HRP into a phosphorescent analog by replacing the heme prosthetic group by Pd-mesoporphyrin. Oxygen readily quenches the phosphorescence of Pd porphyrins, and this can be used to characterize oxygen diffusion
doi:10.1002/prot.10475
pmid:14579357
fatcat:kmoqnr526bdu3oqjcynmktivja