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Eukaryotic Cell, January 2009, p. 47-55, Vol. 8, No. 1
1535-9778/09/$08.00+0 doi:10.1128/EC.00276-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

1*
Department of Parasitology, Charles University, Vini
ná 7, Prague 128 44, Czech Republic,1
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN, 2780-157 Oeiras, Portugal2
Received 18 August 2008/ Accepted 4 November 2008
Trichomonas vaginalis is one of a few eukaryotes that have been found to encode several homologues of flavodiiron proteins (FDPs). Widespread among anaerobic prokaryotes, these proteins are believed to function as oxygen and/or nitric oxide reductases to provide protection against oxidative/nitrosative stresses and host immune responses. One of the T. vaginalis FDP homologues is equipped with a hydrogenosomal targeting sequence and is expressed in the hydrogenosomes, oxygen-sensitive organelles that participate in carbohydrate metabolism and assemble iron-sulfur clusters. The bacterial homologues characterized thus far have been dimers or tetramers; the trichomonad protein is a dimer of identical 45-kDa subunits, each noncovalently binding one flavin mononucleotide. The protein reduces dioxygen to water but is unable to utilize nitric oxide as a substrate, similarly to its closest homologue from another human parasite Giardia intestinalis and related archaebacterial proteins. T. vaginalis FDP is able to accept electrons derived from pyruvate or NADH via ferredoxin and is proposed to play a role in the protection of hydrogenosomes against oxygen.
ná 7, Prague 128 44, Czech Republic. Phone: 420 221951811. Fax: 420 224919704. E-mail: hrdy{at}cesnet.cz
Published ahead of print on 14 November 2008.
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