PhD Studentship: Understanding Heme Enzyme Mechanism Using Dynamic, Time Resolved Crystallography and QM/MM Simulations

The University of Manchester - Department of Chemistry

Application deadline: 23/03/2026
Research theme: Chemistry

This 3.5-year PhD project is fully funded and home students are eligible to apply. The successful candidate will receive an annual tax-free stipend set at the UKRI rate (£20,780 for 2025/26) and tuition fees will be paid. We expect the stipend to increase each year. This is a joint PhD studentship between the University of Manchester and Diamond Light Source, the national synchrotron facility for the UK. The start date is October 2026.

We recommend that you apply early as the advert may be removed before the deadline.

We are seeking candidates for a joint PhD studentship between the University of Manchester and Diamond Light Source, the national synchrotron facility for the UK. The studentship is available for an October 2026 start and is of 3 ½ years duration.

The PhD studentship project will use state-of-the-art experimental structural biology and computational tools to gain a deeper understanding of the environmentally important cytochrome P460 containing enzymes. Time resolved and spectroscopically validated crystal structures of enzyme intermediates will be used synergistically with quantum mechanics/molecular mechanics (QM/MM) computational simulations to understand both the electronic states of enzyme intermediates and the transitions between them.

As a joint studentship, around half of the project will be based in Manchester and half at the Harwell campus in Oxfordshire. The project will also be conducted in collaboration with researchers at STFC Daresbury Laboratory and the University of Bristol. The successful applicant will be based within the groups of and supervised by Prof. Sam Hay (Manchester) and Prof. Mike Hough (Diamond Light Source).

The Hay group are based in the Manchester Institute of Biotechnology (MIB) and Department of Chemistry. A focus of their work is the role of protein dynamics and quantum mechanics during enzyme catalysis. Much of the work involves computational chemistry, often combing molecular dynamics (MD) simulations with enzyme active site density functional theory (DFT) ‘cluster’ or QM/MM models.

The Hough group at Diamond develops methodologies for ambient temperature, time resolved macromolecular crystallography and links these to spectroscopic and computational approaches with the same crystals for validation of redox and ligand states. The group carries out experiments at Diamond and several different X-ray free electron laser facilities.

Contact:

For informal enquiries please contact Sam Hay (Sam.Hay@manchester.ac.uk) or Mike Hough (michael.hough@diamond.ac.uk).

https://www.manchester.ac.uk/research/sam.hay
https://www.diamond.ac.uk/Instruments/Mx/VMXi/Staff/Hough.html

Details of Diamond Light Source and its studentship program may be found here:
https://www.diamond.ac.uk/Home.html
https://www.diamond.ac.uk/Careers/Students/PhD-Studentships.html

Applicants should have, or expect to achieve, at least a 2.1 honours degree or a master’s (or international equivalent) in a relevant science or engineering related discipline.

To apply, please contact the main supervisor, Prof Sam Hay - sam.hay@manchester.ac.uk. Please include details of your current level of study, academic background and any relevant experience and include a paragraph about your motivation to study this PhD project.