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Original scientific paper

ELECTROCHEMICAL INFLUENCE OF NIFUROXAZIDE ON DEHYDROGENASE ACTIVITY

By
Safija Herenda ,
Safija Herenda
Contact Safija Herenda

Faculty of Science, University of Sarajevo , Sarajevo , Bosnia and Herzegovina

Nenad Vanis ,
Nenad Vanis

Asa Hospital Bosnia and Herzegovina

Farzet Bikić ,
Farzet Bikić

University of Zenica

Edhem Hasković
Edhem Hasković

University of Sarajevo

Abstract

Nifuroxazide is an antimicrobial drug from the nitrofuran group, which is used in the treatment of acute bacterial intestinal infections. Its mechanism of action is based on the reduction of the nitro group in bacterial cells, which produces reactive metabolites that permanently damage enzymes and the genetic material of microorganisms. Enzymes of redox metabolism are particularly sensitive, among which lactate dehydrogenase (LDH) stands out. In this work, an electrochemical method (cyclic voltammetry and chronoamperometry) was used to determine kinetic constants. The enzyme LDH (biosensor) was immobilized on a GC electrode and the effect of nifuroxazide on enzyme activity was monitored. The results show that nifuroxazide binds non-competitively to the enzyme and thus changes the enzyme conformation. This process leads to permanent blockade of key metabolic reactions, disruption of the redox balance and death of the bacterial cell.

Conflict of Interest

The authors declare no conflict of interest.

Funding Statement

This research was supported by funding through grant number 05-35-3573-1/25 provided by the Federal Ministry of Education and Science, Sarajevo.

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Authors retain copyright. This work is licensed under a Creative Commons Attribution 4.0 International License. Creative Commons License

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