Peroxidase activity of de novo heme proteins immobilized on electrodes.
De novo proteins from designed combinatorial libraries were bound to heme terminated gold electrodes. The novel heme proteins were shown to possess peroxidase activity, and this activity was compared to that of horseradish peroxidase and bovine serum albumin when immobilized in a similar fashion. The various designed proteins from the libraries displayed distinctly different levels of peroxidase activity, thereby demonstrating that the sequence and structure of a designed protein can exert a substantial effect on the peroxidase activity of immobilized heme.
Das
Aditi
A
Department of Chemistry, Princeton University, Princeton NJ 08544-1009, USA.
Hecht
Michael H
MH
D000818:Animals; D002384:Catalysis; D002417:Cattle; D004563:Electrochemistry / Q000379:methods; D004566:Electrodes; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D006420:Hemeproteins / Q000737:chemistry / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000378:metabolism*; D010545:Peroxides / Q000737:chemistry / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism
D004800:Enzymes, Immobilized; D006420:Hemeproteins; D010545:Peroxides; D012710:Serum Albumin, Bovine; D006735:Horseradish Peroxidase