ISIS Neutron and Muon Source Data Journal

Using the nano discs approach at surfaces to determine the relation between substrate specificity and the conformation of cytochromes P450

Abstract: Membrane bound proteins continue to be to date the most elusive molecules in nature, since they are only functional in the lipid bilayer. We have developed a method to study membrane bound proteins at surfaces using nanodiscs films. We have focused our attention to an enzyme complex producing dhurrin, since this is a model of high value pharmaceutical compounds produced by plants. In particular, we study two cytochrome P450 enzymes that catalyse the reaction of tyrosine into a dhurrin precursor. Despite being very similar in amino-acid structure, they differ largely in substrate specificity. We hypothesise that these differences are due to the specific conformation that the proteins undertake at the lipid membrane. Here we apply neutron reflection and use a series of native and mutant enzymes to corroborate our hypothesis.

Principal Investigator: Professor Marité Cárdenas Gómez
Experimenter: Dr Carmen Domene
Experimenter: Ms Vivien Jagalski
Experimenter: Dr Rob Barker

DOI: 10.5286/ISIS.E.RB1510051

ISIS Experiment Number: RB1510051

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
Select the data format above to find out more about it.

Data Citation

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

For Example:
Professor Marité Cárdenas Gómez et al; (2015): Using the nano discs approach at surfaces to determine the relation between substrate specificity and the conformation of cytochromes P450 , STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1510051

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