Rifampicin is not an inhibitor of tyrosinase

Rifampicin has been previously described as an inhibitor of tyrosinase (Chai et al., Int. J. Biol. Macromol. 102 (2017) 425-430). However, rifampicin contains a p-diphenol group and compounds with such a moiety have been shown before to reduce tyrosinase-generated o-quinones. Rifampicin also shows strong absorption in a region completely overlapping with the visible absorption band of dopachrome, the oxidation product of L -tyrosine and L-dopa, whose concentration is measured spectrophotometrically in the standard enzymatic assay to monitor the activity of tyrosinase. We have demonstrated that rifampicin is also rapidly oxidized by o-quinones generated from catechols by tyrosinase or by treatment with sodium periodate. Smaller changes of absorbance at 475 nm during oxidation of L-dopa by tyrosinase in the presence of rifampicin do not result from enzyme in-hibition but from oxidation of rifampicin by dopaquinone, which leads to rapid decrease of rifampicin absorption in this range. The actual reaction rates are not affected, which we have demonstrated by measurements of oxygen consumption. Rifampicin behaves therefore as other compounds with reducing properties, such as ascorbic acid, hydroquinone, hydrazine derivatives, and flavonoids, some of which have also been incorrectly described before as inhibitors of tyrosinase.

Automated summary

Rifampicin has been found to be both an inhibitor of tyrosinase and can be oxidized by tyrosinase-generated o-quinones. Its absorption overlaps with dopachrome and does not affect the actual reaction rates.