Andjelkovic, AnaOliveira, Marcos T. [UNESP]Cannino, GiuseppeYalgin, CagriDhandapani, Praveen K.Dufour, EricRustin, PierreSzibor, MartenJacobs, Howard T.2018-11-262018-11-262015-12-17Scientific Reports. London: Nature Publishing Group, v. 5, 9 p., 2015.2045-2322http://hdl.handle.net/11449/161054The 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.9engArtigo10.1038/srep18295WOS:000366569400001Acesso abertoWOS000366569400001.pdf