Research Guides

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

Research Interests

The Vincent group are interested in understanding details of catalysis and reactions at metal centres in proteins. 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 carbon monoxide dehydrogenase. We are particularly interested in the efficient catalysis of H₂ oxidation and production by microbial hydrogenase enzymes at [FeFe] or [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 a suite of FTIR surface spectroelectrochemical methods for studying hydrogenase active site chemistry under electrochemical control. Understanding and exploiting selective enzyme catalysis should provide inspiration for new hydrogen energy technologies and development of novel catalytic materials.

One application we have developed and patented is 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.

Kylie Vincent's research is supported by the RCUK, the European Research Council (ERC) and the EPSRC.

Opportunities in the Vincent Group

Informal enquiries about Graduate DPhil opportunities in the group should be directed to K. Vincent. Information about graduate studies at Oxford is available on the Oxford University Graduate Admissions Website.

Up to 4 part II projects for Oxford MChem students will be available in the group for 2013/2014. Email K. Vincent or visit the Vincent group in the Inorganic Chemistry laboratory for further information. Further information about the group is also available on the group webpages.

Lauterbach, L., Idris, Z., Vincent, K.A., Lenz, O. 'Catalytic properties of the isolated diaphorase fragment of the NAD⁺-reducing [NiFe]-hydrogenase from Ralstonia eutropha' PLoS ONE, 2011, 6, (10): e25939.

Lauterbach, L., Liu, J., Horch, M., Hummel, P., Schwarze, A., Haumann, M., Vincent, K.A., Lenz, O., Zebger, I. 'The hydrogenase subcomplex of the NAD⁺-reducing [NiFe]-hydrogenase from Ralstonia eutropha: insights into catalysis and redox interconversions' Eur. J. Inorg. Chem., 2011, 1067-1079.

Healy, A.J., Reeve, H.A., Parkin, A., Vincent, K.A. 'Electrically conducting particle networks in polymer electrolyte as three-dimensional electrodes for hydrogenase electrocatalysis' Electrochimica Acta, 2011, 56, (28) 10786-10790.

Lubner, C.E., Knorzer, P., Silva, P.J.N., Vincent, K.A., Happe,T. , Bryant, D.A., Golbeck, J.H. 'Wiring an [FeFe]-Hydrogenase with Photosystem I for Light-Induced Hydrogen Production' Biochemistry 2010 49 10264–10266.

Healy, A.J., Reeve, H.A., Vincent, K.A. 'Development of an infrared spectroscopic approach for studying metalloenzyme active site chemistry under direct electrochemical control' Faraday Discussions. 2011 148 345 - 357. Presented at Faraday Discussion 148: Spectroscopy, Theory and Mechanism in Bioinorganic Chemistry, 5 - 7 July 2010, University of Nottingham, UK.

Danyal, K., Inglet, B.S., Vincent, K.A., Barney, B.M., Hoffman, B.M., Armstrong, F.A., Dean, D.R., Seefeldt, L.C. 'Uncoupling Nitrogenase: Catalytic Reduction of Hydrazine to Ammonia by a MoFe Protein in the Absence of Fe Protein-ATP' J. Am. Chem. Soc. 132 13197–13199.

Vincent, K.A. 'Triggered Infrared spectroscopy for investigating metalloprotein chemistry' Philosophical Transactions of the Royal Society A (2010) 368, 3713-3731.

Vincent, K.A., Barton, S.C., Canters, G.W., Heering, H.A. 'Electrocatalysis for fuel cells at protein-modified electrodes' in Koper, M. (Ed.) Fuel Cell Catalysis: A Surface Science Approach, John Wiley & Sons, USA, 2009. (Book Chapter)

Ludwig, M., Cracknell, J.A., Vincent, K.A., Armstrong, F.A., Lenz, O. 'Oxygen-Tolerant H₂ Oxidation By Membrane-Bound [NiFe]-Hydrogenases of Ralstonia species: Coping with Low-Level H₂ in Air' J. Biol. Chem. (2009) 284, 465-477.

Cracknell, J.A., Vincent, K.A., Armstrong, F.A. 'Enzymes as Working or Inspirational Electrocatalysts for Fuel Cells and Electrolysis' Chem. Rev. (2008) 108, 7, 2439-2461.

Vincent, K.A., Parkin, A., Armstrong, F.A. 'Investigating and exploiting the electrocatalytic properties of hydrogenases' Chem. Rev. (2007) 107, 10, 4366-4413.