I studied Physics Engineering at Politecnico di Milano (Milano, Italy), where I earned a bachelor’s degree followed by a master’s degree. Both of them consisted mainly of solid state physics classes, with a particular focus on semiconductors (for electronics and photonics application) and magnetic nanostructures. My first experience in research was at the European Synchrotron Radiation Facility (Grenoble, France), where I spent 10 months working as a trainee for my master thesis project.
Read more about Davide Pincini
Brief project description:
This project addresses key challenges in X-ray absorption spectroscopy studies of metal- containing proteins, namely how to control and protect against photoreduction and X-ray damage and how to generate protein samples in well-defined oxidation states. These questions are highly relevant on beamlines like I20, where the high intensity allows study of low protein concentrations (typical for biological studies) but in turn is more likely to induce damage to the protein. Exploiting expertise of Vincent and Ash in Oxford on electrochemical control of metalloproteins, we explore the applicability of a pulsed solution electrochemical flow approach, demonstrated by Best, to protect proteins during room temperature solution measurements of defined redox states. We will set up this approach on the I20 beamline and aim to generate data on a range of metalloprotein sites which will serve as models for understanding XAS of more complex enzymes.
This will include electron transfer proteins with haem and non-haem iron sites, copper and nickel sites and an iron-sulphur cluster, as well as the bimetallic NiFe catalytic centre of hydrogenase. We then extend the study to a direct electrochemical approach in which the protein of interest is immobilised on a carbon electrode and exchanges electrons directly, enabling fast catalytic oxidation and reduction reactions in an enzyme to be controlled in situ during XAS measurement. This will enable us to explore the interesting question of whether an electrode can function as a ‘sink’ for X-ray generated photoelectrons over a range of potentials, thus maintaining the proteins in a controlled oxidation state and protecting against damage. If successful, these studies will have broad applicability in bio-inorganic chemistry and bring the UK to the forefront of XAS studies of metalloproteins.
This studentship is linked with the BBSRC Oxford Interdisciplinary Bioscience Doctoral Training Partnership.
Applications to this studentship will open in early 2018.
Diamond Light Source Ltd. holds an Athena SWAN Bronze Award, demonstrating their commitment to provide equal opportunities and to advance the representation of women in STEM/M subjects: science, technology, engineering, mathematics and medicine.
Diamond Light Source is the UK's national synchrotron science facility, located at the Harwell Science and Innovation Campus in Oxfordshire.
Copyright © 2017 Diamond Light Source
Diamond Light Source Ltd
Harwell Science & Innovation Campus