Why are absorbance values in the presence of an inhibitor lower than in the absence?
Understand the Problem
The question is asking about the effect of an inhibitor on absorbance values in a biochemical or chemical context. It seeks to understand why the presence of an inhibitor results in lower absorbance readings compared to when the inhibitor is absent, implying the need for a relationship between absorbance, the substance being measured, and the inhibitor's action.
Answer
Inhibitors lower absorbance by decreasing enzyme activity and reducing product formation.
The presence of an inhibitor lowers absorbance values because it reduces the enzyme's ability to catalyze the reaction, which decreases product formation and consequently lowers absorbance.
Answer for screen readers
The presence of an inhibitor lowers absorbance values because it reduces the enzyme's ability to catalyze the reaction, which decreases product formation and consequently lowers absorbance.
More Information
Inhibition decreases enzyme activity, lowering product formation which is detected as absorbance, a method used in enzyme kinetics to track reaction progress.
Tips
A common mistake is assuming inhibitors increase absorbance due to binding; however, their primary effect is reducing enzyme catalysis.
Sources
- 5.4: Enzyme Inhibition - Chemistry LibreTexts - chem.libretexts.org
- Enzymes: principles and biotechnological applications - PMC - pmc.ncbi.nlm.nih.gov
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