Year
2018
Degree Name
Doctor of Philosophy
Department
School of Chemistry
Abstract
Bioluminescence in marine systems is dominated by the use of one ligand for light production, coelenterazine. The bioluminescent reaction of coelenterazine is an enzyme catalysed, oxidative decarboxylation. During the reaction coelenterazine reacts with molecular oxygen to form carbon dioxide, coelenteramide and light. One such class of bioluminescent systems is the Ca[sup]2+-regulated photoproteins. These proteins, rather than continuously processing substrate, bind 2-hydroperoxycoelenterazine as an intermediate along the reaction pathway. The reaction is halted here until an external stimulus triggers the continuation of the bioluminescent reaction. There are currently no reported experimental, atomistic descriptions of the states that lead to this ternary michaelis complex. This study utilises computational techniques to develop an atomistic description of the complex of coelenterazine with one photoprotein, obelin.
Recommended Citation
Griffiths, Thomas M., Atomistic insights into photoprotein formation: computational prediction of the properties of coelenterazine and oxygen binding in Obelin, Doctor of Philosophy thesis, School of Chemistry, University of Wollongong, 2018. https://ro.uow.edu.au/theses1/326
FoR codes (2008)
0103 NUMERICAL AND COMPUTATIONAL MATHEMATICS, 0204 CONDENSED MATTER PHYSICS, 0307 THEORETICAL AND COMPUTATIONAL CHEMISTRY
Unless otherwise indicated, the views expressed in this thesis are those of the author and do not necessarily represent the views of the University of Wollongong.