Issue 3, 2004
From the journal:

Chemical Communications

An inorganic iron complex that inhibits wild-type and an isoniazid-resistant mutant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis

Jaim S. Oliveira,a   Eduardo H. S. Sousa,b   Luiz A. Basso,*a   Moisés Palaci,c   Reynaldo Dietze,c   Diógenes S. Santosd  and  Ícaro S. Moreira*b  

* Corresponding authors

a Universidade Federal do Rio Grande do Sul, Departamento de Biologia Molecular e Biotecnologia, Av. Bento Gonçalves 9500, Porto Alegre, RS 91501-970, Brazil
E-mail: labasso@dna.cbiot.ufrgs.br

b Universidade Federal do Ceará, Departamento de Química Orgânica e Inorgânica, Campus Pici, Fortaleza, CE 60455-760, Brazil
E-mail: icarosm@dqoi.ufc.br

c Universidade Federal do Espírito Santo, Núcleo de Doenças Infecciosas, Av. Marechal Campos 1468, Vitória, ES 29040-091, Brazil

d Faculdade de Farmácia, Instituto de Pesquisas Biomédicas, Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, CEP 90619-900, Brazil
E-mail: diogenes@dna.cbiot.ufrgs.br

Abstract

The in vitro kinetics of inactivation of both wild-type and I21V InhA enzymes by [FeII(CN)5(INH)]3− indicate that this process requires no activation by KatG, and no need for the presence of NADH. This inorganic complex may represent a new class of lead compounds to the development of anti-tubercular agents aiming at inhibition of a validated target.

Graphical abstract: An inorganic iron complex that inhibits wild-type and an isoniazid-resistant mutant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis

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Article information

DOI
https://doi.org/10.1039/B313592F
Article type
Communication
Submitted
28 Oct 2003
Accepted
24 Nov 2003
First published
07 Jan 2004

Chem. Commun., 2004, 312-313

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An inorganic iron complex that inhibits wild-type and an isoniazid-resistant mutant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis

J. S. Oliveira, E. H. S. Sousa, L. A. Basso, M. Palaci, R. Dietze, D. S. Santos and Í. S. Moreira, Chem. Commun., 2004, 312 DOI: 10.1039/B313592F

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