Laura Edit Barabás

Abstract Human carbonic anhydrase II (hCAII) is a reported biocatalyst for stereoselective reduction of aryl-alkyl-substituted ketones using phenylsilane as an abiotic hydride ion source. During studies investigating the substrate scope of hCAII/PhSiH3, we examined the reduction of 1-phenyl-1,2-propanedione under different conditions. In the presence of 2–6 equivalents of PhSiH3, we unexpectedly observed exclusive formation of enantiopure anti/syn-1-phenylpropane-1,2-diols (PPDs).

1 Introduction In nature, enzymes function cooperatively within metabolic pathways to convert carbon sources into energy and essential building blocks [1, 2]. Inspired by these biological systems, industrial biocatalysis has increasingly adopted nature-inspired strategies to enhance process efficiency and selectivity [3-6]. Within this framework, multienzyme cascades have emerged as powerful tools for modern chemical manufacturing [7], enabling streamlined synthetic routes [8-10].