Publication: Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
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Date
2015-12-17
Advisor
Coadvisor
Graduate program
Undergraduate course
Journal Title
Journal ISSN
Volume Title
Publisher
Nature Publishing Group
Type
Article
Access right
Acesso aberto
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.
Description
Keywords
Language
English
Citation
Scientific Reports. London: Nature Publishing Group, v. 5, 9 p., 2015.
