Peroxidase activity of de novo heme proteins immobilized on electrodes

被引：43

作者：

Das, Aditi ^{[1
]}

Hecht, Michael H. ^{[1
]}

机构：

[1] Princeton Univ, Dept Chem, Princeton, NJ 08544 USA

来源：

JOURNAL OF INORGANIC BIOCHEMISTRY | 2007年 / 101卷 / 11-12期

关键词：

protein design; binary patterning; cyclic voltammetry; redox protein; heme protein; peroxidase activity; horseradish peroxidase; chronocoulometry;

D O I：

10.1016/j.jinorgbio.2007.07.024

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1820 / 1826

页数：7

共 39 条

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[Anonymous], CURR SEP

[2] Combinatorial and computational challenges for biocatalyst design [J].