This research program is concerned with the basic question of the mechanism of energy conversion in biological organisms, specifically how the luminous bacteria channel their metabolic energy into light. This reaction is called Bioluminescence, and results of these studies are finding increasing applications, for example to clinical diagnostics. It is known that the reaction is an oxidation of fatty aldehyde involving riboflavin phosphate and an enzyme called luciferase. The particular reaction mechanism is very challenging to-scientists because it has been so elusive. In a major genus of the bacteria called Photobacterium, we discovered the """"""""antenna"""""""" that radiates the light. This is a protein which we call Lumazine Protein and its structure and interactions are the subject of the main NIH-supported grant. The collaboration with the Institute of Biophysics in Krasnoyarsk (USSR), is mainly concerned with the luciferase, its structure and reaction mechanism, but also we enlist their help with some non-overlapping aspects of the lumazine protein project, since these proteins are tightly linked in the overall mechanism in the cell. In Krasnoyarsk they will produce single point mutations of luciferase determine residues important for catalysis and interaction with lumazine protein. The mutated subunits will be produced for testing for separate function and to produce crystals for X-ray structure determination. No structures of these proteins have ever been obtained. This collaboration will lead to significant advance in knowledge of metabolic processes in bacteria leading to development of antibiotics and diagnostics.
