Dr Philip Ash

Supervisor Details

Contact Details

School of Chemistry, University of Leicester

Scientific Background

Research Interests

My research group is interested in developing novel biophysical tools for studying catalysis at metal centres within proteins. Of particular importance are enzymes that catalyse activation of small molecules such as dihydrogen (H2), carbon monoxide, carbon dioxide, and dinitrogen (N2). The chemistry that occurs at enzyme active sites is inspirational for production and use of future sustainable fuels. Active sites are often based around ‘inorganic’ cores similar to naturally-occurring minerals, and can be studied using a range of spectroscopic techniques. In combination with electrochemistry, it is possible to use spectroscopy to build up 'snapshots' of enzyme reactivity in situ during catalysis. At present we are involved in developing novel room-temperature methods for X-ray absorption spectroscopy, and time-resolved infrared spectroscopy. A deeper mechanistic understanding of how nature has developed efficient enzymes will provide inspiration for the next generation of biomimetic catalysts for green energy and synthesis. My research is supported by the Royal Society, Royal Society of Chemistry, Science and Technology Funding Council, Diamond Light Source, BBSRC, and EPSRC.

Supervision Style

In three words or phrases: Supportive, detail-oriented, collaborative

Provision of Training

Initial training will be carried out by myself, sometimes in collaboration with other experienced group members. You will then become more independent, and take the lead in carrying out method development and refinement.

Progression Monitoring and Management

We will discuss goals regularly and review technical developments and results in detail every two weeks (or as appropriate), in addition to our normal day-to-day interactions in the lab.

Communication

I do occasionally send emails over evenings and weekends, but do not expect a response. We will occasionally undertake experiments at national facilities, where some evening/weekend working is required, but I strongly support taking time off to mitigate/recover! Work-life balance is important, and you should feel free to manage this in a way that works for you.

PhD Students can expect scheduled meetings with me:

In a group meeting

At least once per fortnight

In year 1 of PhD study

At least once per fortnight

In year 2 of PhD study

At least once per month

In year 3 of PhD study

At least once per month

These meetings will be a mixture of face to face or via video chat or telephone, and I am usually contactable for an instant response on every working day.

Working Patterns

The timing of work in my lab is completely flexible, and (other than attending pre-arranged meetings), I expect students to manage their own time.

Notice Period for Feedback

I need at least 1 week’s notice to provide feedback on written work of up to 5000 words.

Project Details

Dr Ash is the supervisor on the below project:

Chemical energy conversion in biology studied using advanced spectroscopic and structural tools

Secondary Supervisor(s): Dr Hannah Kwon

University of Registration: University of Leicester

BBSRC Research Themes:

Renewable Resources and Clean Growth (Bio-energy)
Understanding the Rules of Life (Structural Biology)

Apply here!

Deadline: 4 January, 2024

Project Outline

Redox properties of metal-containing active sites are critically important to many biocatalytic processes: one third of all proteins contain a redox-active metal, and ca 22% of submissions to the Protein Data Bank contain a transition metal. Metalloproteins capable of extracting energy from H2 gas, sequestering CO2 from the atmosphere, or performing complex monooxygenation reactions, rely upon the ability to access and control a range of often exotic metal oxidation states in an aqueous environment. Much of this crucial chemistry occurs at extremely fast rates, making it challenging to study using conventional structural and spectroscopic methods.

This project aims to investigate the catalytic mechanisms and structural dynamics of metalloenzymes that are vital for chemical energy conversion, with a focus on hydrogenase. State-of-the-art spectroscopic and structural studies will be combined with computational analysis to reveal critical but elusive transient intermediates by studying reactions in real time on sub-microsecond timescales. The outcomes of this project will provide a step change in our understanding of the mechanism of hydrogenase and other metalloenzymes, and will serve as inspirational catalysts for future green energy technologies.

A PhD student will gain a broad range of interdisciplinary skills in spectroscopy, electrochemistry, chemical biology, structural biology, and biophysics whilst addressing critical questions about how nature achieves efficient chemical energy conversion.

Techniques

Molecular Biology (cloning & mutagenesis)
Protein expression and purification
X-ray Spectroscopy
Time-resolved spectroscopy (infrared, Raman)
Synchrotron science
Chemical synthesis
Enzyme kinetics
Protein crystallisation
Structure determination

Dr Ash is also the co-supervisor on a project with Dr Hanna Kwon.

Previous Projects

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