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Review
. 2010;10(12):11530-55.
doi: 10.3390/s101211530. Epub 2010 Dec 15.

Nitrite biosensing via selective enzymes--a long but promising route

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Review

Nitrite biosensing via selective enzymes--a long but promising route

M Gabriela Almeida et al. Sensors (Basel). 2010.

Abstract

The last decades have witnessed a steady increase of the social and political awareness for the need of monitoring and controlling environmental and industrial processes. In the case of nitrite ion, due to its potential toxicity for human health, the European Union has recently implemented a number of rules to restrict its level in drinking waters and food products. Although several analytical protocols have been proposed for nitrite quantification, none of them enable a reliable and quick analysis of complex samples. An alternative approach relies on the construction of biosensing devices using stable enzymes, with both high activity and specificity for nitrite. In this paper we review the current state-of-the-art in the field of electrochemical and optical biosensors using nitrite reducing enzymes as biorecognition elements and discuss the opportunities and challenges in this emerging market.

Keywords: biosensors; electrochemical transducers; nitrite; nitrite reductases.

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Figures

Figure 1.
Figure 1.
Schematic representations of the working principles of different enzymatic nitrite biosensors. Mediated amperometric transduction: (a) mediator and enzyme are co-immobilized on the matrix film; (b) mediator is entrapped on the working electrode material; (c) enzyme and physiological mediator linked to a DNA modified electrode. (d) Direct electrochemical transduction; (e) Potentiometric transduction; (f) Conductimetric transduction; (g) Optical transduction (medox—mediator in the oxidized form; medred—mediator in the reduced form; NiRox—NiR oxidized state; NiRred—NiR reduced state; dithionite (S2O42−) works as reducing equivalents source).
Figure 1.
Figure 1.
Schematic representations of the working principles of different enzymatic nitrite biosensors. Mediated amperometric transduction: (a) mediator and enzyme are co-immobilized on the matrix film; (b) mediator is entrapped on the working electrode material; (c) enzyme and physiological mediator linked to a DNA modified electrode. (d) Direct electrochemical transduction; (e) Potentiometric transduction; (f) Conductimetric transduction; (g) Optical transduction (medox—mediator in the oxidized form; medred—mediator in the reduced form; NiRox—NiR oxidized state; NiRred—NiR reduced state; dithionite (S2O42−) works as reducing equivalents source).
Figure 2.
Figure 2.
Cyclic voltammograms recorded with a Nafion/ccNiR/methyl viologen/GCE biosensor in the absence of nitrite and in the presence of various nitrite concentrations; adapted from [30]. Inset: corresponding calibration curve.
Figure 3.
Figure 3.
Three-dimensional structures of nitrite reductases. (a) Desulfovibrio vulgaris Hildenborough multiheme c nitrite reductase (NrfA4NrfH2 complex); the catalytic subunit (NrfA) is depicted in blue and the electron donor subunit (NrfH) in gray; heme groups are shown in dark red [65]. (b) Spinach nitrite reductase; siroheme is shown in dark red and iron-sulfur cluster in yellow [70]. (c) Achromobacter cycloclastes copper nitrite reductase (trimer); the copper centres are shown in blue [71]. (d) Pseudomonas aeruginosa cytochrome cd1 nitrite reductase (dimer); heme c is depicted in dark red and heme d in blue [72].

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