Dr Philip Ash

Lecturer in Chemistry

School/Department: Chemistry, School of

Telephone: +44 (0)116 294 4561



I am a graduate of Wadham College, University of Oxford (MChem). I completed my PhD research in the group of Professor Colin Bain (Durham University) where I used a range of physical methods to study phase transitions in mixed monolayers of surfactant and alkane. My PhD research involved collaborative work at the Royal Institute of Technology (KTH Stockholm) supported by a Rideal Travel Bursary. I carried out postdoctoral research at the University of Oxford with Professor Kylie Vincent where I received support from the John Fell Fund and a Researcher Mobility Grant (Royal Society of Chemistry) to undertake collaborative work with Dr. Hans-Petter Hersleth at the University of Oslo. In 2019 I took up a lectureship in the School of Chemistry at the University of Leicester where I am also associated with the Leicester Institute of Structural and Chemical Biology. I am currently a member of the Science and Technology Funding Council’s Life Sciences and Soft Materials Advisory Panel.


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.



  1. P. A. Ash, S. E. T. Kendall-Price, R. M. Evans, S. B. Carr, A. R. Brasnett, S. Morra, J. S. Rowbotham, R. Hidalgo, A. J. Healy, G. Cinque, M. D. Frogley, F. A. Armstrong, K. A. Vincent, The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase, Chem. Sci. 2021, 12, 12959-12970.
  2. S. Morra et al., Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site, Dalton Trans. 2021, 50, 12655-12663.
  3. S. P. Best, V. A. Streltsov, C. T. Chantler, W. Li, P. A. Ash, S. Diaz-Moreno,  Redox state and photoreduction control using X-ray spectroelectrochemical techniques - advances in design and fabrication through additive engineering, J. Synchrotron Rad. 2021, 28, 472-479.
  4. P. A. Ash, S. E. T. Kendall-Price, K. A. Vincent, Unifying activity, structure and spectroscopy of [NiFe] hydrogenases: combining techniques to clarify mechanistic understanding, Acc. Chem. Res. 2019, 52, 3120-3131.
  5. D. B. Grabarczyk. P. A. Ash, W. K. Myers, E. L. Dodd, K. A. Vincent, Dioxygen controls the nitrosylation reactions of a protein-bound [4Fe4S] cluster, Dalton Trans. 2019, 48, 13960-13970.
  6. R. M. Evans, P. A. Ash, S. E. Beaton, E. K. Brooke, K. A. Vincent, S. B. Carr, F. A. Armstrong, Mechanistic exploitation of a self-repairing, blocked proton transfer pathway in an O2-tolerant [NiFe]-hydrogenase, J. Am. Chem. Soc. 2018, 140, 10208-10220.
  7. P. A. Ash, R. Hidalgo, K. A. Vincent, Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase, J. Vis. Exp. 2017, 130, e855858.
  8. P. A. Ash, S. B. Carr, H. A. Reeve, A SkorupskaitÄ—, J. S. Rowbotham, R. Shutt, M. D. Frogley, G. Cinque, F. A. Armstrong, K. A. Vincent, A method for generating single metalloprotein crystals in well-defined redox states: combined electrochemical control and infrared microspectroscopic imaging of a NiFe hydrogenase crystal, Chem. Commun. 2017, 53, 5858-5861.
  9. P. A. Ash et al., Proton transfer in the catalytic cycle of NiFe hydrogenases: insight from vibrational spectroscopy, ACS Catal. 2017, 7, 2471-2485.
  10. Ash, P. A., Vincent, K. A., 'Vibrational Spectroscopic Techniques for Probing Bioelectrochemical Systems' in 'Biophotoelectrochemistry: From Bioelectrochemistry to Biophotovoltaics', Volume 158 of the series 'Advances in Biochemical Engineering / Biotechnology', pp 75-110, Springer, 2016.


I supervise research students on projects involving bioinorganic chemistry, biocatalysis, biomimetic catalysis, and biophysical method development. A particular focus is on redox enzymes involved in small molecule activation. I am always interested in hearing from potential research students, PDRAs, or collaborators.


I am actively involved in teaching on all degrees offered by the School of Chemistry, undertaking a range of laboratory demonstration, tutorials, problem classes, and lectures. I also supervise undergraduate (BSc and MChem) and postgraduate research project students. I am module convenor of CH3202 (Advanced Inorganic Chemistry) and lecture on CH4208 (Bioinorganic Chemistry). I am a Fellow of the Higher Education Academy (FHEA).

Press and media

I am happy to provide opinion on research at large national facilities, enzyme chemistry, bioinspired chemistry, electrocatalysis, green energy, hydrogen production, and related topics. I have collated a range of short videos detailing research within Leicester that are available via the School of Chemistry.
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