Journal
NEW BIOTECHNOLOGY
Volume 54, Issue -, Pages 71-79Publisher
ELSEVIER
DOI: 10.1016/j.nbt.2019.08.005
Keywords
P450; Human P450 substrates; Peroxide shunt; Peroxygenase activity; Diclofenac; Tamoxifen
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The heme domain of cytochrome P450 116B5 from Acinetobacter radioresistens (P450 116B5hd), a self-sufficient class VII P450, was functionally expressed in Escherichia coli, purified and characterised in active form. Its unusually high reduction potential (-144 +/- 42 mV) and stability in the presence of hydrogen peroxide make this enzyme a good candidate for driving catalysis with the so-called peroxide shunt, avoiding the need for a reductase and the expensive cofactor NAD(P)H. The enzyme is able to carry out the peroxide-driven hydroxylation of aromatic compounds such as p-nitrophenol (K-M = 128.85 +/- 29.51 mu M and k(cat) = 2.65 +/- 0.14 min(-1)), 10-acetyl-3,7-dihydroxyphenoxazine (K-M = 6.01 +/- 0.32 mu M and k(cat) = 0.33 +/- 0.03 min(-1)), and 3,5,3', 5'tetramethylbenzidine (TMB). Moreover, it catalyses different reactions on well-known drugs such as hydroxylation of diclofenac (K-M = 49.60 +/- 6.30 mu M and k(cat) = 0.06 +/- 0.01 min(-1)) and N-desmethylation of tamoxifen (K-M = 57.20 +/- 7.90 mu M and k(cat) = 0.79 +/- 0.04 min(-1)). The data demonstrate that P450 116B5hd is an efficient biocatalyst for sustainable applications in bioremediation and human drug metabolite production.
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