Research Guides

Department of Chemistry University of Oxford

Professor Kylie Vincent

Visit the group webpages for further information: http://vincent.chem.ox.ac.uk/

The Vincent group is currently seeking applications from interested candidates for a 3-year funded DPhil Studentship on 'Mechanistic studies of NiFe hydrogenases', and we will shortly be seeking applications for a 4-year BBSRC iCASE funded DPhil Studentship on 'Biocatalytic hydrogenation in flow'. Informal enquiries about these posts can be directed to Prof. Kylie Vincent. To be eligible for these positions, candidates must meet the UK Research Councils’ residency criteria.

Research Interests

The Vincent group are interested in understanding details of catalysis and reactions at metal sites, both in enzymes and on metal nanoparticles relevant to fuel cell catalysis. Redox enzymes play key roles as catalysts in biological cycling of hydrogen, carbon and nitrogen and energy. Their active sites are built from common metals such as iron, nickel and copper, and the reactivity achieved at these centres is often difficult to replicate under ambient conditions with synthetic catalysts. We are interested in understanding details of the redox chemistry and mechanisms of catalysis occurring at enzyme active sites. A central theme in our research is attachment of enzymes to electrically conducting surfaces (electrodes or conducting particles). This provides precise control over enzyme reactions in direct electrochemical and spectroelectrochemical studies, but it also provides an immediate route to applying biological redox catalysis in hydrogen technologies and in specialised catalysis. 

Our studies target a range of metalloproteins including hydrogenases, nitrogenase and nitric oxide sensing proteins. We are particularly interested in the efficient catalysis of H2 oxidation and production by microbial hydrogenase enzymes at [NiFe] active centres. Ligands at the active site of hydrogenases, CO and CN-, give rise to fairly intense absorption bands in the Infrared spectrum. This has inspired us to develop new approaches to infrared spectroelectrochemistry for studying hydrogenase active site chemistry under direct electrochemical control. Understanding and exploiting selective enzyme catalysis will provide inspiration for new hydrogen energy technologies and development of novel catalytic materials.

We have demonstrated and patented a system for recycling the biological cofactors NAD(P)+ and NAD(P)H with H2 as electron source or sink using graphite particles modified with enzyme moieties. We are developing this further to support catalysis by a wide range of NAD(P)H dependent enzymes, including keto reductases, ene reductases and monooxygenases, and are working in collaboration with industry to develop enzyme beads for industrial chemical synthesis.

Kylie Vincent's research is supported by the EPSRC and the BBSRC.

Opportunities in the Vincent Group

The Vincent group is currently advertising for a Postdoctoral Research Associate in Flow Chemistry to support research and development related to our HydRegen biocatalysis platform. Further information is available from the Departmental Job Vacancies Website

Informal enquiries about Postdoctoral Fellowship applications, Graduate DPhil (PhD) or MSc opportunities or Undergraduate Summer Studentships in the group should be directed to Prof Kylie Vincent. General information about graduate studies at Oxford is available on the Oxford University Graduate Admissions Website. We are always happy to hear from candidates interested in applying for their own scholarship or fellowship funding to work in the group.

The Vincent group will take 3-4 Part II Oxford MChem students for 2017/2018. Email Kylie Vincent for further information about future Part II projects. Further information about the group is also available on the group webpages.

Paengnakorn, P., Ash, P.A., Shaw, S., Danyal, K., Chen, T., Dean, D.R., Seefeldt, L.C., Vincent, K.A., 'Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding', Chemical Science, 2016, DOI:10.1039/C6SC0286.

McPherson, I.J., Ash, P.A, Jacobs, R.M.J., Vincent, K.A. 'Formate adsorption on Pt nanoparticles during formic acid electro-oxidation: insights from in situ infrared spectroscopy', Chem. Commun., 2016, 52, 12665-12668.

Ash, P.A, Reeve, H.A., Quinson, J., Hidalgo, R., Zhu, T., McPherson, I.J., Chung, M., Healy, A.J., Nayak, S., Lonsdale, T.H., Wehbe, K., Kelley, C.S., Frogley, M.D., Cinque, G., Vincent, K.A. 'Synchrotron-based Infrared Microanalysis of Biological Redox Processes under Electrochemical Control' Anal. Chem., 2016, 88, 6666

Reeve, H.A., Lauterbach, L., Lenz, O., Vincent, K.A. 'Enzyme-Modified Particles for Selective Bio-Catalytic Hydrogenation via H2-driven NADH Recycling' ChemCatChem, 2015, 7, 21, 3480.   

Ash, P.A., Liu, J., Coutard, N., Heidary, N., Horch, M., Gudim, I., Simler, T., Zebger, I., Lenz, O., Vincent, K.A., 'Electrochemical and Infrared Spectroscopic Studies Provide Insight into Reactions of the NiFe Regulatory Hydrogenase from Ralstonia eutropha with O2 and CO' J. Phys. Chem. B, 2015, 119, 13807-13815

Murphy, B.J., Hidalgo, R., Roessler, M.M., Evans, R.M., Ash, P.A., Myers, W.K., Vincent, K.A., Armstrong, F.A. 'Discovery of Dark pH-Dependent H+ Migration in a [NiFe]-hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate' J. Am. Chem. Soc. 2015, 137, 26, 8484–8489.
 
Duca, M., Weeks, J.R., Fedor, J.G., Weiner, J.H., Vincent, K.A. 'Combining Noble Metals and Enzymes for Relay Cascade Electrocatalysis of Nitrate Reduction to Ammonia at Neutral pH' ChemElectroChem 2015, 2, 1086-1089.
 
Hidalgo, R., Ash, P.A., Healy, A.J., Vincent, K.A. 'Infrared Spectroscopy During Electrocatalytic Turnover Reveals the Ni-L Active Site State During H2 Oxidation by a NiFe Hydrogenase' Angew. Chemie Int. Ed. 2015, 127, 7216-7219.
 
Grabarczyk, D.B., Ash, P.A., Vincent, K.A. 'Infrared Spectroscopy Provides Insight into the Role of Dioxygen in the Nitrosylation Pathway of a [2Fe2S] Cluster Iron-Sulfur Protein' J. Am. Chem. Soc., 2014, 136, 11236-11239.