RESEARCH

Protein Design
We are interested in the design of novel proteins. This field has been accelerated by the recent development of deep-learning structure prediction tools, starting with Alphafold2. Our previous work included the development of a synthetic beta-solenoid protein (SynRFR) and derivatives. We are now using deep learning methods to design novel solenoid proteins and other novel proteins, including ligand binding proteins.

Carbon Fixation
We are interested in carbon fixation in plants and cyanobacteria, and how it may be improved. To this end we have several structural projects in proteins involved in carbon fixation. We are also using flux balance to model carbon fixation metabolism in cyanobacteria. Recent work includes the cryoEM structure of the GAPDH-CP12-PRK complex, and the crystal structure of acetone carboxylase.

Light Reactions
We have moved into using cryoEM to study the structures of the pigment-protein complexes involved in the light reactions of photosynthesis. In collaboration with the Rutherford group, we are looking at the structures of the far-red chl f containing photosystems.

Photosystem II
Photosystem II (PSII) is the membrane protein-pigment complex which uses visible light photons to drive the oxidation of water (H2O), to oxgyen (O2), protons and electrons. After other reactions, the electrons are used to drive the reduction of carbon dioxide to organic molecules. Photosystem II generates almost all of the oxygen in the atmosphere, and is ultimately responsible for the fixation of most of the biomass, and fossil fuels on the Earth. Without PSII, the Earth would be much less hospitable to life. Apart from its intrinsic biological interest, replicating artificially the reaction of Photosystem II is vital for developing "artificial photosynthesis", the use of sunlight to generate fuels.

We are studying ways to mimic the catalytic activity of photosystem II by engineering other proteins to bind a cluster of metal atoms in a similar way to the natural system. We are also working on the structures of proteins related to the assembly and repair of the PSII reaction centre.

Nitrogenase
In plants, electrons from photosynthesis are added to carbon dioxide in the Calvin cycle to fix carbon. Another important reduction is that of nitrogen to ammonia by the nitrogenase enzyme. Nitrogenase is complex, with three structural proteins, and many more assembly factors. We are investigating the structural basis of nitrogenase resistance to oxygen, which is important for biotechnological applications of this enzyme.



Education/Qualifications:
DPhil, University of Oxford (2005) 
BA, MSci, University of Cambridge (2000)