Bioluciferase, with no presence of mitochondria, is highly reactive among ATP, but altering pH levels results in denaturing.
Abstract.
By measuring how different reagents affect the luciferin and luciferase mixture, called lantern, we will show the importance of the energy contained in ATP as well as other reagents like ADP and GTP. Reactions, here, will occur due to enzyme specificity. If the active site of the lantern can be fit with the substrates we add, energy will be released in the form of light. We will then see how altering pH levels will affect the lantern by adding an acid as well as a base. NADH will be added to another tube to see how it will affect the lantern. NADH builds in mitochondria, and mitochondria helps to make ATP. So, by adding NADH, if there is a reaction we know that there are mitochondria present in the lantern. We filled seven vials with lantern and then added the reagents. Once all groups added all components to the vials we turned off the lights to see the light energy released. We rated our observances on a scale from zero to five, zero being no light omitted and five being very bright. We concluding that ATP produced the most light, ADP producing the next largest amount. Next, ATP plus a base and also GTP (both observed in only one group) produced a tiny amount of light, and NADH, ATP plus an acid, and plain lantern producing no light. We observed some group variations and minor differences in results. Conclusions rested that ATP, with its high energy bonds and specific shape, produced the highest level of light energy. Shape was key and the ATP obviously fit the best into the lantern's active site. All of the other reagents did not fit well into the active site of the lantern, therefore producing little or no light energy.
Introduction.
This experiment's purpose was to show the importance of the energy contained in the molecule adenosine triphosphate (ATP) within an enzyme substrate reaction.
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