Halogenation of estrogens catalysed by a fungal chloroperoxidase

Abstract

Chloroperoxidase (CPO) is a haeme-thiolate enzyme able to catalyse the halogenation and oxidation of a wide range of organic substrates. In this work, the CPO-catalysed chlorination and bromination reaction of natural estrogens was characterised. Estradiol, estrone and equiline were efficiently converted to halogenated compounds in the presence of chloride or bromide and hydrogen peroxide. The catalytic efficiency of CPO in this reaction is similar to that measured for other aromatic substrates; as expected the bromination reaction proceeds more efficiently than the chlorination reaction. Three major products were detected for chlorination of estradiol; two of them were monohalogenated compounds while a third product was a dihalogenated compound at positions 2 and 4 of the aromatic ring A. Chlorinated compounds are not substrates for tyrosinase, suggesting that the halogenated form of estrogens is less susceptible to form o-quinones.

Keywords:

• Biotransformation
• chloroperoxidase
• estradiol
• estrogen
• halogenation
• unspecific peroxygenase

Acknowledgements

The authors thank Fernando González for technical support with semipreparative HPLC.

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

This research was supported by UNAM-DGAPA under grant PAPIIT IN209116.