|Photosynthetic organisms provide us with food and other materials by using light energy from the sun to capture carbon dioxide from the atmosphere to make usable sugars. Almost all CO2 enters the biosphere via the enzyme ribulose-1,5-bisphosphate carboxylase oxygenase (Rubisco). In spite of the crucial importance of this process Rubisco is non-specific and slow, which has forced nature to hugely overexpress the protein, or to use tricks such as biochemical or biophysical carbon concentrating mechanisms to saturate the enzyme with substrate. |
Genomic studies have uncovered that Nature possesses a great diversity of Rubiscos and associated protein machinery to perform the task of CO2 capture, much of it poorly characterized. Research in my laboratory aims to mechanistically describe the biochemistry of CO2-fixation related machinery. By increasing our understanding of the sophisticated mechanisms that have evolved in remote branches of the tree of life, we hope to provide knowledge that can later be applied to improving the photosynthetic efficiency of crop species.
An emerging interest concerns the use of cyanobacteria as a synthetic biology platform. This involves both the utilization and implementation of heterologous CO2 fixation machinery, as well as the potential to channel the photosynthate towards compounds of scientific and commercial interest.
- Shivhare D, Mueller-Cajar O. (2017). In Vitro Characterization of Thermostable CAM Rubisco Activase Reveals a Rubisco Interacting Surface Loop. Plant Physiology, 174(3), 1505-1516.
- Jin S, Sun J, Wunder T, Tang D, Cousins AB, Sze SK, Mueller-Cajar O, Gao YG. (2016). Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases.. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 113(51), 14716-14721.
- Loganathan N, Tsai YC, Mueller-Cajar O. (2016). Characterization of the heterooligomeric red-type rubisco activase from red algae. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 113(49), 14019-14024.
- Tsai Y.C., Lapina M.C., Bushan S., Mueller-Cajar O. (2015). Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria. Nature Communications, 6, 8883.
- Durão P, Aigner H, Nagy P, Mueller-Cajar O, Hartl FU, Hayer-Hartl M. (2015). Opposing effects of folding and assembly chaperones on evolvability of Rubisco.. Nature Chemical Biology, 11(2), 148-55.