Title: Towards Rational Mutation of an Enzyme: Understanding Rubisco's Specificity

Speaker: Dr. Jurgen Schlitter, University Unknown—Look up or ask Paul

Date/Time: Wednesday, May 18, 2005, 10:30-11:30 am

Location: Building 980, Room 95 (Sandia NM)

Brief Abstract: The plant enzyme Rubisco plays a prominent role in photosynthesis as it fixes gaseous carbon dioxide to Ribulose molecules, thus being the main material entry of the biosphere. During evolution it developed increasing specificity for carbon dioxide as compared to oxygen binding which opens an energetically unfavorable pathway. Our today’s understanding of this interesting progress started with comparative studies of sequences which indicated the importance of the C-terminal tail and led us to successful mutational experiments. The later developed time-window hypothesis connects the kinetics of the conformational change that opens the binding niche with the specificity of the binding process. Recent MD simulations support the hypothetical correlation between structure, conformational kinetics and specificity. It seems possible now to predict beforehand semi-quantitatively the specificity of new mutants.

CSRI POC: Paul Crozier, (505) 845-9714