Rebecca Gregory

The Key to a biofuel future: unravelling the mechanism of GH61

My research involves the structural and mechanistic determination of a class of polysaccharide degrading metalloproteins (Lytic Polysaccharide Monooxygenases, LPMOs), known as AA10s (see  These enzymes are copper dependent and are able to oxidatively degrade polysaccharides, such as chitin and cellulose.  AA10s are found naturally in bacteria, and my project involves looking at the structures of a number of these enzymes, as well as determining their mechanistic action and substrate specificity.  Various techniques will be used, such as crystallography and EPR spectroscopy to analyse the structures.  MALDI-Mass Spectrometry will be used to determine the activity of the enzymes on various substrates, and redox chemistry will help determine the oxidative mechanistic pathway.  These LPMO enzymes have great potential for the biotechnology industry, as they greatly enhance the classical enzymatic degradation of plant biomass and may contribute to the production of biofuels.

I obtained my MChem degree in Chemistry from the University of York.  I spent my final year abroad at the University of Helsinki, Finland, where I carried out my final year project in Organic Chemistry with Professor Kristiina Wähälä.  My PhD research is with Professors. Gideon Davies and Paul Walton.


  • The Copper Active Site of CBM33 Polysaccharide Oxygenases.
    G. R. Hemsworth, E. J. Taylor, R. Q. Kim, R. C. Gregory, S. J. Lewis, J. P. Turkenburg, A. Parkin, G. J. Davies and P. H. Walton.  J Am Chem Soc. 2013, 135, 6069-6077.