Interaction of human dihydroorotate dehydrogenase with ubiquinone and dihydroorotate in mimics of the inner mitochondrial membrane
Human dihydroorotate dehydrogenase (DHODH) is an integral membrane protein found in the inner mitochondrial membrane (IMM). DHODH is a flavoenzyme that catalyzes the oxidation of dihydroorotic acid (DHO) with the simultaneous reduction of ubiquinone (coenzyme Q10). DHODH is a well-validated drug target for the treatment of autoimmune disorders. In addition, mutations in the DHODH gene are the cause of Miller Syndrome, a Mendelian disorder characterized by abnormalities of the head and limbs. DHODH consists of a mitochondrial signal (MS), a transmembrane helix domain (TM), two amphipathic alpha helices and a catalytic domain. We propose to continue our investigation of the interaction between the soluble form of DHODH (lacking the MS and TM segments) and supported lipid bilayers consisting of natural phospholipid mixtures derived from yeast (instead of synthetic lipids) mimicking the composition of the IMM. The bilayers will incorporate Q10 (either hydrogenous or partially deuterated). Finally, the soluble substrate (DHO) will be added to determine whether substrate addition results in changes in the location and conformation of the enzyme and Q10.
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KNECHT Wolfgang; BOGOJEVIC Oliver; DELHOM Robin; FRAGNETO Giovanna; OROZCO RODRIGUEZ Juan Manuel and WACKLIN KNECHT Hanna. (2019). Interaction of human dihydroorotate dehydrogenase with ubiquinone and dihydroorotate in mimics of the inner mitochondrial membrane. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-858
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