Dr Philip Ash
Supervisor Details
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.
Research Groups
Metalloenzyme mechanism with sub-turnover frequency time resolution
MIBTP Project Details
Previous Projects (2024-25)
Primary supervisor for:
Co-supervisor on a project with Dr Hanna Kwon.
Previous Projects (2023-24)
Primary supervisor for: