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The malaria parasite type IINADH : quinone oxidoreductase: an alternative enzyme for an alternative lifestyle

Fisher, Nicholas, Bray, Patrick, Ward, Stephen ORCID: https://orcid.org/0000-0003-2331-3192 and Biagini, Giancarlo ORCID: https://orcid.org/0000-0001-6356-6595 (2007) 'The malaria parasite type IINADH : quinone oxidoreductase: an alternative enzyme for an alternative lifestyle'. Trends in Parasitology, Vol 23, Issue 7, pp. 305-310.

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Abstract

The operation of a type II NADH:quinone oxidoreductase (PfNDH2), also known as alternative Complex I, in the mitochondrion of the human malaria parasite, Plasmodium falciparum, has recently been described. Unlike the Complex I of typical mitochondria, type II NADH:quinone oxidoreductases do not have transmembrane domains and are not involved directly in proton (H+) pumping. Here, we present a predictive model of PfNDH2, describing putative NADH-, flavin- and quinone-binding sites, as well as a possible membrane 'anchoring' region. In addition, we hypothesize that the alternative Complex I is an evolutionary adaptation to a microaerophilic lifestyle enabling (proton) uncoupled oxidation of NADH. This adaptive feature has several advantages, including: (i) a reduction of proton 'back-pressure' in the absence of extensive ATP synthesis; (ii) a reduction of mitochondrial superoxide generation; and (iii) a mechanism for the deregulated oxidation of cytosolic NADH.

Item Type: Article
Uncontrolled Keywords: nadh-ubiquinone oxidoreductase plasmodium-falciparum oxidative-phosphorylation superoxide-production respiratory-chain electron-transfer escherichia-coli binding-sites complex-i mitochondria
Subjects: QX Parasitology > Protozoa > QX 135 Plasmodia
WC Communicable Diseases > Tropical and Parasitic Diseases > WC 750 Malaria
Faculty: Department: Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group
Digital Object Identifer (DOI): https://doi.org/10.1016/j.pt.2007.04.014
Depositing User: Ms Julia Martin
Date Deposited: 01 Sep 2010 11:10
Last Modified: 06 Feb 2018 13:01
URI: https://archive.lstmed.ac.uk/id/eprint/1193

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