Biology: The Structure Of Luciferase Essay

1880 words - 8 pages

Proteins play a fundamental role in the existence of living organisms. They are major contributors of cell structure and mobility, hormonal interaction, information exchange, and, most importantly, regulation of essential reactions. Enzymes are proteins that activate or inhibit the conversion of a substrate to a product. Often, enzymes catalyze reactions that are crucial for biological processes, but a few regulate other aspects of life, such as communication between a species. The enzyme luciferase catalyzes the reaction that allows fireflies to communicate with each other via emission of a yellow-green to yellow-orange colored light (Nakatsu, T. et al., 2006, 372). This reaction is a bioluminescence reaction, where chemical energy is converted into light energy (Branchini, B.R., Magyar, R.A., Murtiashaw, M.H., and Portier, N.C, 2001, 2410). Luciferase stimulates an interesting reaction mechanism that is dependent on the enzyme’s structure and environmental factors, resulting in varying colors of emitted light. Furthermore, luciferase, though mainly found in insects, has practical application in cancer monitoring and research for humans.
The structure of luciferase makes it part of the ‘acyl-adenylate/thioester-forming’ family of enzymes. The distinguishing quality of the family is an enormous N-terminus domain, housing the major portion of the activation site comprised of residues 1-436, and an exponentially smaller C-terminus domain, made up of residues 440-550 (Branchini, B.R., Magyar, R.A., Murtiashaw, M.H., and Portier, N.C, 2001, 2411). The enzyme changes its conformation upon substrate binding; the gap between the N-terminus and C-terminus, also known as the active site, closes to increase the enzyme’s efficiency in creating a product – refer to Appendix B for active site model (Thorne, N., Inglese, J., Auld, D.S., 2010, 650). The substrate that binds to the active site of luciferase is luciferin, which is converted to oxyluciferin through a series of reactions to emit light ranging from yellow-green to red. The excited-state product releases light in the form of photons as it returns to a ground-state conformation (Nakatsu, T. et al., 2006, 372). Yellow-green light represents the production of a high-energy excited state compound, whereas red light is the result of a low energy excited state molecule (Branchini, B.R., Magyar, R.A., Murtiashaw, M.H., and Portier, N.C, 2001, 2411).
The luciferase-catalyzed reaction begins with the binding of the luciferin to the active site of the enzyme. Luciferase tightly anchors the benzothiazole ring of luciferin to the phenolic oxygen of the luciferin-binding site, via hydrogen bonding or cation-pi interactions, to prevent the rotation of the substrate (Branchini, B.R., Magyar, R.A., Murtiashaw, M.H., and Portier, N.C, 2001, 2417). The proper binding of the luciferin substrate is critical, as loose binding may result in rotation, which does not maximize excited states of...

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