ATP-dependent hydroxylation of an unactivated primary carbon with water

Christian Jacoby, Sascha Ferlaino, Dominik Bezold, Henning Jessen, Michael Müller and Matthias Boll ()
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Christian Jacoby: Albert-Ludwigs-Universität Freiburg
Sascha Ferlaino: Albert-Ludwigs-Universität Freiburg
Dominik Bezold: Albert-Ludwigs-Universität Freiburg
Henning Jessen: Albert-Ludwigs-Universität Freiburg
Michael Müller: Albert-Ludwigs-Universität Freiburg
Matthias Boll: Albert-Ludwigs-Universität Freiburg

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Enzymatic hydroxylation of unactivated primary carbons is generally associated with the use of molecular oxygen as co-substrate for monooxygenases. However, in anaerobic cholesterol-degrading bacteria such as Sterolibacterium denitrificans the primary carbon of the isoprenoid side chain is oxidised to a carboxylate in the absence of oxygen. Here, we identify an enzymatic reaction sequence comprising two molybdenum-dependent hydroxylases and one ATP-dependent dehydratase that accomplish the hydroxylation of unactivated primary C26 methyl group of cholesterol with water: (i) hydroxylation of C25 to a tertiary alcohol, (ii) ATP-dependent dehydration to an alkene via a phosphorylated intermediate, (iii) hydroxylation of C26 to an allylic alcohol that is subsequently oxidised to the carboxylate. The three-step enzymatic reaction cascade divides the high activation energy barrier of primary C–H bond cleavage into three biologically feasible steps. This finding expands our knowledge of biological C–H activations beyond canonical oxygenase-dependent reactions.

Date: 2020
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DOI: 10.1038/s41467-020-17675-7

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