Journal article

Publication year: 2008

Pages: 2731-2742

Journal: Organic & Biomolecular Chemistry

Volume number: 6

Issue number: 15

ISSN: 1477-0520

eISSN: 1477-0539

DOI Link: https://doi.org/10.1039/b802649c

Publisher: Royal Society of Chemistry

Abstract: 
Various aza-analogues of 1,4-naphthoquinone and menadione were prepared and tested as inhibitors and substrates of the plasmodial thioredoxin and glutathione reductases as well as the human glutathione reductase. The replacement of one to two carbons at the phenyl ring of the 1,4-naphthoquinone core by one to two nitrogen atoms led to an increased oxidant character of the molecules in accordance with both the redox potential values and the substrate efficiencies. Compared to the 1,4-naphthoquinone and menadione, the quinoline-5,8-dione 1 and both quinoxaline-5,8-diones 5 and 6 behaved as the most efficient subversive substrates of the three NADPH-dependent disulfide reductases tested. Modulation of these parameters was observed by alkylation of the aza-naphthoquinone core.

Harvard Citation style: Morin, C., Besset, T., Moutet, J., Fayolle, M., Brückner, M., Limosin, D., et al. (2008) The aza-analogues of 1,4-naphthoquinones are potent substrates and inhibitors of plasmodial thioredoxin and glutathione reductases and of human erythrocyte glutathione reductase, Organic and Biomolecular Chemistry, 6(15), pp. 2731-2742. https://doi.org/10.1039/b802649c

APA Citation style: Morin, C., Besset, T., Moutet, J., Fayolle, M., Brückner, M., Limosin, D., Becker, K., & Davioud-Charvet, E. (2008). The aza-analogues of 1,4-naphthoquinones are potent substrates and inhibitors of plasmodial thioredoxin and glutathione reductases and of human erythrocyte glutathione reductase. Organic and Biomolecular Chemistry. 6(15), 2731-2742. https://doi.org/10.1039/b802649c