Peroxidase activity of de novo heme proteins immobilized on electrodes

Aditi Das, Michael H. Hecht

Research output: Contribution to journalArticlepeer-review

49 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1820-1826
Number of pages7
JournalJournal of Inorganic Biochemistry
Issue number11-12
StatePublished - Nov 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry


  • Binary patterning
  • Chronocoulometry
  • Cyclic voltammetry
  • Heme protein
  • Horseradish peroxidase
  • Peroxidase activity
  • Protein design
  • Redox protein


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