Sunday, 15 October 2006
Salon E - H (Doubletree Hotel at Reid Park)
401

Protein Conformational Changes in Energy Transfer in the Reaction Centers of Purple Bacteria

Christa Laser, Arizona State University Biodesign Institute, Tempe, AZ

The study of photosynthesis is the primary pathway that humans have to increasing the efficiency of the collection of renewable solar power. But, photosynthesis does not just take place in plants. In fact, it is often easier to study the proteins involved in transfer of electrons during photosynthesis by studying bacteria. The photosynthetic reaction center in purple bacteria was long thought to be a completely stationary protein which facilitated a quick electron transfer without conformational change, since the transfer of electrons occurred at very fast speeds. However, by mutating this bacteria at specific sites related to the structure of the reaction center, the exact method by which electron transfer occurs has been better illuminated. A mutation at M203, from a glycine to a leucine, was produced in this purple bacteria, sterically removing a water molecule from between the bacteriochlorophyll and the bacteriopheophytin, two of several cofactors of the reaction center. The reaction centers were isolated. Then, the speed of the electron transfer was compared to that of the unmutated, wild type, reaction center. The results showed that the speed of electron transfer was greatly reduced, yet still occurred. This added to the results of other mutations to support a theory that the electron transfer is dependant upon the motion of the protein. This may have significant impact on the further study of photosynthesis, the better understanding of which may benefit renewable energy production in the future.

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