Creation of synthetic catalysts with enzyme-like behavior is challenging despite strong interest in such systems. Extraction of tetrachloroaurate into the hydrophilic core of an interfacially cross-linked reverse micelle (ICRM) produced an artificial “metalloenzyme” with highly unusual catalytic properties. The ICRM pulled the substrate toward the catalytic metal, which converted it efficiently to the product that was rapidly ejected. These features enabled greatly reduced catalyst loading (30–100 times lower than typical levels used in literature examples), constant high reaction rate throughout the course of the reaction, lack of the hydrolyzed side product, and substrate selectivity unobserved in conventional gold catalysts.