Peroxidase activity of de novo heme proteins immobilized on electrodes

Aditi Das; Michael H. Hecht

doi:10.1016/j.jinorgbio.2007.07.024

Peroxidase activity of de novo heme proteins immobilized on electrodes

Aditi Das, Michael H. Hecht

Research output: Contribution to journal › Article › peer-review

49 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	1820-1826
Number of pages	7
Journal	Journal of Inorganic Biochemistry
Volume	101
Issue number	11-12
DOIs	https://doi.org/10.1016/j.jinorgbio.2007.07.024
State	Published - Nov 2007

All Science Journal Classification (ASJC) codes

Biochemistry
Inorganic Chemistry

Keywords

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

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10.1016/j.jinorgbio.2007.07.024

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title = "Peroxidase activity of de novo heme proteins immobilized on electrodes",

abstract = "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.",

keywords = "Binary patterning, Chronocoulometry, Cyclic voltammetry, Heme protein, Horseradish peroxidase, Peroxidase activity, Protein design, Redox protein",

author = "Aditi Das and Hecht, {Michael H.}",

note = "Funding Information: This work was supported by the NIH Grant R01 GM062869 (M.H.H.). A.D. acknowledges FMC Graduate fellowship. The authors are grateful to Dr. Scott A. Trammell and Prof. Andrew B. Bocarsly for helpful discussions. We further thank Prof. John T. Groves for the use of the potentiostat. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",

year = "2007",

month = nov,

doi = "10.1016/j.jinorgbio.2007.07.024",

language = "English (US)",

volume = "101",

pages = "1820--1826",

journal = "Journal of Inorganic Biochemistry",

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T1 - Peroxidase activity of de novo heme proteins immobilized on electrodes

AU - Das, Aditi

AU - Hecht, Michael H.

N1 - Funding Information: This work was supported by the NIH Grant R01 GM062869 (M.H.H.). A.D. acknowledges FMC Graduate fellowship. The authors are grateful to Dr. Scott A. Trammell and Prof. Andrew B. Bocarsly for helpful discussions. We further thank Prof. John T. Groves for the use of the potentiostat. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

PY - 2007/11

Y1 - 2007/11

N2 - 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.

AB - 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.

KW - Binary patterning

KW - Chronocoulometry

KW - Cyclic voltammetry

KW - Heme protein

KW - Horseradish peroxidase

KW - Peroxidase activity

KW - Protein design

KW - Redox protein

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JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

IS - 11-12

ER -

Peroxidase activity of de novo heme proteins immobilized on electrodes

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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