Abstract
Pentachlorophenol (PCP) is a persistent chemical contaminant that has been extensively investigated in terms of its toxicology and metabolism. Similar to PCP, other chlorinated phenol derivatives are also widely present in the environment from various sources. Even though some of the chlorine-substituted phenols, and particularly PCP, are well-known inhibitors of phenol sulfotransferases (SULTs), these compounds have been shown to undergo sulfation in humans. To investigate the enzymatic basis for sulfation of PCP in humans, we have studied the potential for PCP as well as the mono-, di-, tri-, and tetra-chlorinated phenols to serve as substrates for human hydroxysteroid sulfotransferase, hSULT2A1. Our results show that all of these compounds are substrates for this isoform of sulfotransferase, and the highest rates of sulfation are obtained with PCP, trichlorophenols, and tetrachlorophenols. Much lower rates of sulfation were obtained with isomers of monochlorophenol and dichlorophenol as substrates for hSULT2A1. Thus, the sulfation of polychlorinated phenols catalyzed by hSULT2A1 may be a significant component of their metabolism in humans.
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