Journal
JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 101, Issue 11-12, Pages 1820-1826Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2007.07.024
Keywords
protein design; binary patterning; cyclic voltammetry; redox protein; heme protein; peroxidase activity; horseradish peroxidase; chronocoulometry
Funding
- NIGMS NIH HHS [R01 GM062869-04, R01 GM062869] Funding Source: Medline
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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. (c) 2007 Elsevier Inc. All rights reserved.
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