Oliver Mueller-Cajar



Nanyang Assistant Professor
Division of Structural Biology and Biochemistry

Office: SBS-02n-17
Telephone: 6592 3184
Email: cajar@ntu.edu.sg



  • B.Sc.,Hons (First Class), University of Canterbury, New Zealand
  • Ph.D., Australian National University, Australia


I undertook my PhD studies under the supervision of Dr. Spencer Whitney at the Australian National University in Canberra, studying the artificial evolution of the photosynthetic CO2-fixing enzyme Rubisco. Subsequently I joined the laboratory of Dr. Manajit Hayer-Hartl at the Max-Planck Institute of Biochemistry near Munich, Germany, where I discovered a novel molecular motor that activates Rubisco. My group at NTU started in August 2012.

Research Interest

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 CO2 pumps 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 existing in nature we hope to provide knowledge that can later be applied to improving the photosynthetic efficiency of crop species.


A, The CO2-fixing enzyme Rubisco needs to be activated by CO2 and Mg2+ cofactors. In the absence of the cofactors the substrate ribulose 1,5-bisphosphate (RuBP) binds to and inhibits the enzyme. A Rubisco activase is required to release the inhibitor.
B, Mechanistic model of Rubisco activation by the novel Rubisco activase CbbX. The ring-shaped activase transiently pulls on the C-terminus of the Rubisco large subunit, resulting in active site opening and release of the inhibitor.