ISIS Neutron and Muon Source Data Journal

Interaction of human dihydroorotate dehydrogenase with ubiquinone in model lipid bilayers

Abstract: Human dihydroorotate dehydrogenase (DHODH) is a membrane-bound enzyme of clinical interest and a well-validated drug target for e.g. rheumatoid arthritis and multiple sclerosis. The exact way in which DHODH interacts with membrane-bound ubiquinone (coenzyme Q10) and with inhibitors is not known. Our goal is to use investigate the mechanisms by which DHODH interacts with ubiquinone, with lipids and with inhibitors in planar lipid bilayers mimicking the composition of the inner mitochondrial membrane. We have carried out preliminary neutron reflectivity experiments at the ILL to investigate the structure of supported lipid bilayers made from synthetic lipids and yeast membranes containing ubiquinones Q2 and Q10. The aim of this experiment is to study the interaction of the catalytic domain of DHODH with ubiquinones Q2 and Q10 in model lipid bilayers.

Principal Investigator: Dr Wolfgang Knecht
Experimenter: Dr Hanna Wacklin-Knecht
Experimenter: Mr Juan Manuel Orozco Rodriguez
Experimenter: Mr Robin Delhom
Local Contact: Dr Maxmilian Skoda

DOI: 10.5286/ISIS.E.RB1820287

ISIS Experiment Number: RB1820287

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Wolfgang Knecht et al; (2018): Interaction of human dihydroorotate dehydrogenase with ubiquinone in model lipid bilayers, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1820287

Data is released under the CC-BY-4.0 license.