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

• DOI: 10.1038/srep18295
• Publication Date: 2015-12-17T11:23:48Z
• Authors: Ana Andjelković; Marcos T. Oliveira; Giuseppe Cannino; Cagri Yalgin; Praveen K. Dhanda...; Eric Dufour; Pierre Rustin; Marten Szibor; Howard T. Jacobs
• Keywords: Alternative oxidase

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 AOX from Ciona instestinalis , carrying mutations at conserved residues predicted to be required for chelation diiron prosthetic group. protein was stably expressed mammalian cells or flies, but lacked enzymatic activity unable rescue phenotypes flies knocked down subunit cytochrome oxidase. mutated transgene is thus potentially useful tool studies physiological effects expression.