The Chemistry of Bioluminescence: An Analysis of Chemical Functionalities
AlbaNova and Nordita Colloquium 2011
Wednesday 25 January 2012
to 12:00 at
Roland Lindh (Uppsala University)
Firefly luciferase is one of the most studied bioluminescent system. It has been extensively studied both theoretically and experimentally. Based on these studies we will herein give a review on the current understanding of the bioluminescent process from a chemical functionality perspective. This presentation will emphasize three key components: the chemiluminophore, the electron-donating fragment and how these are affected by the substrate-enzyme interaction. The understanding is based on details of how the peroxide -O-O- bond supports the production of electronically excited products and how the Charge Transfer Induced Luminescent, CTIL, mechanism, with the aid of an electron-donating group, lowers the activation barrier, to support a reaction in living organisms. For the substrate-enzyme complex it is demonstrated that the enzyme can affect the hydrogen-bonding around the CTIL controlling group resulting in a mechanism for color modulation. Finally, in the light of the purpose of the fragments of the luciferin-luciferase complex to provide key chemical functionalities we will analyse other luciferin-luciferase systems with respect to similarities and differences.
If time available I will discuss the significance of the difference between the chemiluminescent and fluorescent states of luciferin and its implications for theoretical and experimental investigations.