Professor Michael Danson
My fundamental research programme aims to understand the structural basis of extremophile enzyme stability and catalytic activity, in particular to temperature and salinity. My experimental approaches include molecular enzymology, molecular biology, X-ray crystallography, site-directed mutagenesis and directed evolution.
I am also interested in the biotechnological application of enzymes from extremophiles, exploiting their high stabilities to, and activities in, extreme conditions. Many extremophiles belong to the Archaea, an evolutionary-distinct domain in addition to the Eukarya and Bacteria. Archaea are known to possess unusual metabolic features, and therefore I am also aiming to exploit their enzymes that have unique catalytic specificities. Part of this programme involves the isolation, from environmental samples, of novel extremophilic micro-organisms according to their metabolic and enzymic capabilities.
This citrate synthase enzyme comes from Pyrococcus, an archeaon that grows optimally at 100oC.
Clicking on the image will show an animation of how the subunits of the molecule move during catalysis.