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• Yarman, A
• Neumann, B
• Bosserdt, M
• Gajovic-Eichelmann, N
• Scheller, F
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• Yarman, A
• Neumann, B
• Bosserdt, M
• Gajovic-Eichelmann, N
• Scheller, F
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• Yarman, A
• Neumann, B
• Bosserdt, M
• Gajovic-Eichelmann, N
• Scheller, F

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Biosensors 2012, 2(2), 189-204; doi:10.3390/bios2020189

Article

Peroxide-Dependent Analyte Conversion by the Heme Prosthetic Group, the Heme Peptide “Microperoxidase-11” and Cytochrome c on Chitosan Capped Gold Nanoparticles Modified Electrodes

Aysu Yarman, Bettina Neumann, Maria Bosserdt, Nenad Gajovic-Eichelmann and Frieder W. Scheller *

Fraunhofer Institute for Biomedical Engineering, IBMT, D-14476 Potsdam, Germany

* Author to whom correspondence should be addressed.

Received: 10 April 2012; in revised form: 3 May 2012 / Accepted: 9 May 2012 / Published: 14 May 2012

(This article belongs to the Special Issue Electrochemical Based Biosensors)

Download PDF Full-Text [397 KB, uploaded 14 May 2012 08:20 CEST]

Abstract: In view of the role ascribed to the peroxidatic activity of degradation products of cytochrome c (cyt c) in the processes of apoptosis, we investigate the catalytic potential of heme and of the cyt c derived heme peptide MP-11 to catalyse the cathodic reduction of hydrogen peroxide and to oxidize aromatic compounds. In order to check whether cyt c has an enzymatic activity in the native state where the protein matrix should suppress the inherent peroxidatic activity of its heme prosthetic group, we applied a biocompatible immobilization matrix and very low concentrations of the co-substrate H₂O₂. The biocatalysts were entrapped on the surface of a glassy carbon electrode in a biocompatible chitosan layer which contained gold nanoparticles. The electrochemical signal for the peroxide reduction is generated by the redox conversion of the heme group, whilst a reaction product of the substrate oxidation is cathodically reduced in the substrate indication. The catalytic efficiency of microperoxidase-11 is sufficient for sensors indicating HRP substrates, e.g., p-aminophenol, paracetamol and catechol, but also the hydroxylation of aniline and dehalogenation of 4-fluoroaniline. The lower limit of detection for p-aminophenol is comparable to previously published papers with different enzyme systems. The peroxidatic activity of cyt c immobilized in the chitosan layer for catechol was found to be below 1 per mill and for p-aminophenol about 3% as compared with that of heme or MP-11.

Keywords: peroxide dependent catalysis; hemin; microperoxidase-11; cytochrome c

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