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Laboratoire d'Electrochimie Moleculaire, LEM, Paris

UMR CNRS - Université Paris Diderot - Paris France

   
 
Master Frontiers in Chemistry | UFR de Chimie - Université Paris Diderot - Paris 7 CNRS - Institut de chimie Université de Paris Master Chimie Sorbonne Paris Cité UFR de Chimie - Université Paris Diderot - Paris 7 CNRS - Institut de chimie
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Université Paris Diderot
Université de Paris CNRS, Centre National de la Recherche Scientifique
 
 


Le LEM - Publications: Abstracts

Publication 540

Analyst, 126 (6), 887-891, 2001
DOI: 10.1039/b100533m
 

 


Determination of horseradish peroxidase and a peroxidase-like iron porphyrin at a Nafion-modified electrode

Chantal Degrand, Benoît Limoges, Anne-Marie Martre and Bernd Schöllhorn

Contribution from the Laboratoire d'Electrochimie Moléculaire, Unité Mixte de Recherche Université - CNRS No 7591, Université de Paris 7 - Denis Diderot, 2 place Jussieu, 75251 Paris Cedex 05, France


A catalytic coupling reaction between 4-amino antipyrine and a N,N-disubstituted aniline derivative has been exploited in the indirect electrochemical detection of horseradish peroxidase (HRP) and of a biomimetic catalyst, the iron(iii) sulfonated tetraphenyl porphyrin. In the presence of hydrogen peroxide and one of the two catalysts a cationic electroactive quinone-iminium dye P+ was formed and detected by linear scan voltammetry using a screen-printed electrode coated with a Nafion film. Detection limits of 10-12 M for HRP and 4 × 10-10 M for the iron porphyrin have been achieved. In conclusion the iron porphyrin is considered to be a promising alternative to the HRP label in enzyme immunoassays with electrochemical detection.

 
   
 
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