We combine evolutionary, computational, sequence-structure-function (x-ray crystallography, serial-femtosecond crystallography), biochemistry, and synthetic biology approaches to address our research questions.
Rubisco isoforms can be found in a diverse range of phylogenetically distinct organisms, including leafy green plants, algae, bacteria, and even archaea. These different Rubisco isoforms have evolved under very different selection pressures, and may exhibit “weird” kinetics, assembly pathways, thermotolerance, or other strange properties. We look for exotic Rubisco sequence-structure, in order to harness unique and beneficial CO2-fixing strategies.
The structure and function of “red” Rubiscos found in red algae and diatoms diverges from that of “green” Rubiscos found in leafy plants. Red Rubiscos are much more efficient than green Rubiscos, but the reason for their remarkable kinetics is unknown. We aim to harness naturally superior red Rubisco kinetics, using structural biology, protein engineering and synthetic biology approaches.
Higher plants (with “green” Rubiscos) contain auxiliary subunits called “small” subunits. Plants contain multiple small subunit isoforms, which are differentially expressed in response to a variety of environmental cues. This project aims to characterise and take advantage of the contribution of different auxiliary subunits to Rubisco assembly and activity.
We use Molecular Dynamics simulations to identify sequence-structure that channels the correct substrate to the active site in Rubisco. Molecular Dynamics analysis of a diverse range of Rubiscos from different evolutionary lineages will be combined with sequence-structure information to identify amino acids that contribute to enhanced substrate selectivity.