Scientists Successful in Synthesizing Rubisco

Researchers at the Max Planck Institute of Biochemistry and the Gene Center of Ludwig Maximilians University Munich report that they have succeeded in rebuilding Rubisco, an enzyme that plays a linchpin role in photosynthesis. Rubisco, one of the most important proteins in nature, catalyzes the conversion of atmospheric carbon dioxide to organic compounds in photosynthesis. "But this process is really inefficient", explains Manajit Hayer-Hartl, a group leader at the MPI of Biochemistry. "Rubisco not only reacts with carbon dioxide but also quite often with oxygen."  This did not cause any problems with the protein developed three billion years ago. Back then, there was no oxygen present in the atmosphere. However, as more and more oxygen accumulated, Rubisco could not adjust to this change.

Rubisco has been the target of scientists working to in improve crop yield and control greenhouse gas-induced climate change. Up to now, the enzyme's complex structure made it impossible to reconstruct it in the laboratory. To overcome this problem, Hayer-Hartl and colleagues used molecular chaperones. These chaperones make sure that the protein folds the right way and acquires it s correct three-dimensional structure. The researchers showed that two different chaperone systems, called GroEL and RbcX, are necessary to produce a functional Rubisco complex. They are now working to genetically modify Rubisco so that it binds more carbon dioxide and reacts less with oxygen.

The complete paper published by Nature is available to subscribers at http://dx.doi.org/10.1038/nature08651 Read http://www.mpg.de/english/illustrationsDocumentation/documentation/pressReleases/2010/
pressRelease20100112/index.html for more information.