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Reduction of Different Nitro‐Compounds on Electroenzymatic System: Cytochrome c Reductase‐NAD(P)H Modified Carbon Paste Electrode
Author(s) -
Merino M.,
NuñezVergara L. J.,
Squella J. A.
Publication year - 1999
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/(sici)1521-4109(199911)11:17<1285::aid-elan1285>3.0.co;2-t
Subject(s) - nitrobenzene , chemistry , nitro , electrode , cyclic voltammetry , redox , nad+ kinase , reductase , inorganic chemistry , nuclear chemistry , nitro compound , electrochemistry , organic chemistry , enzyme , catalysis , alkyl
A flavoenzyme cytochrome c reductase NAD(P)H mixture has been used to modify a carbon paste electrode. The modified electrode was characterized by cyclic voltammetry varying the scan rate and temperature. Cathodic and anodic peaks were observed at –0.45 and –0.39 V, respectively, for a scan rate of 100 mV/s. The enzyme‐electrode is found to reduce electrocatalytically nitroimidazole and nitrofurane compounds. However, this effect was not observed on the reduction of nitrobenzene derivatives such as nitrobenzene substituted 1,4‐dihydropyridines. Conditions such as pH and percentage of DMF have been optimized for the determination of these nitro‐compounds. The best electrocatalytic reactions were obtained at pH 8.5, coincident with the optimal activity of the enzyme.