Discussion
Why is ultraviolet absorption used to follow enzyme reactions?
Answer: A
Cofactors such as the reduced nicotinamide dinucleotide absorb strongly at 340 nanometres while their oxidised forms do not, so the reaction's progress appears directly as a changing absorbance. Proteins absorb weakly near 280 rather than in the visible, and neither heat nor refractive index is being measured. Following a reaction through a species whose absorption changes is the general pattern, and it needs no sampling, no quenching and no separation. A single measurement chosen to respond to the one asymmetry beats several that respond to shared behaviour.
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