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Sci Rep. 2015 Dec 17;5:18295. doi: 10.1038/srep18295.

Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies.

Author information

1
BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland.
2
Departamento de Tecnologia, Faculdade de Ciências Agrárias e Veterinárias, Universidade Estadual Paulista "Júlio de Mesquita Filho", 14884-900 Jaboticabal, SP, Brazil.
3
Institute of Biotechnology, University of Helsinki, FI-00014, Finland.
4
INSERM UMR 1141 and Université Paris 7, Faculté de Médecine Denis Diderot, Hôpital Robert Debré, 48, Boulevard Sérurier, 75019, Paris, France.

Abstract

The mitochondrial alternative oxidase, AOX, carries out the non proton-motive re-oxidation of ubiquinol by oxygen in lower eukaryotes, plants and some animals. Here we created a modified version of AOX from Ciona instestinalis, carrying mutations at conserved residues predicted to be required for chelation of the diiron prosthetic group. The modified protein was stably expressed in mammalian cells or flies, but lacked enzymatic activity and was unable to rescue the phenotypes of flies knocked down for a subunit of cytochrome oxidase. The mutated AOX transgene is thus a potentially useful tool in studies of the physiological effects of AOX expression.

PMID:
26672986
PMCID:
PMC4682143
DOI:
10.1038/srep18295
[Indexed for MEDLINE]
Free PMC Article

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