Gunn lab

We study and engineer nature’s vital, but notoriously inefficient CO2-fixing enzyme, Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), whose catalysis limits the growth of crop plants and cyanobacteria used for biofuel production.We look for ways to develop the prerequisite information and tools to express more efficient Rubisco variants in crops and cyanobacteria: by identifying unique structure-function, overcoming chaperone incompatibilities, and understanding and utilizing the catalytic influence of the auxiliary Rubisco small subunit.

Popular science presentation

Watch our "2 minute" popular science presentation on youtube for an easily accessible introduction to our research.

Read more about expressing red Rubsico in Green Plants here and here.

Research projects

We combine evolutionary, computational, sequence-structure-function (x-ray crystallography, serial-femtosecond crystallography), biochemistry, and synthetic biology approaches to address our research questions.

Weird Rubiscos
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.

Red Rubisco
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.

Green Rubisco
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.

Computational studies
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.

People

Laura Gunn, PhD
Group Leader

Afshan Begum, PhD
Researcher

Former members

Stavros Azinas, PhD
Postdoctoral researcher

Frida Boström, Masters student

Shruti Ravi, masters student

Natalia Reynisdottir, intern​

  • Estelle Pignon, masters student
  • Ivo van den Hurk, intern
  • Celia da Luz, masters student
  • Josefin Ågren, intern
  • Sara Rönnblad-Ericsson, intern
  • Pushkar Chitale, masters student

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