The substrate specificity of chloroperoxidase from Caldaromyces fumago in a number of halide-independent reactions was investigated and the ability of this enzyme to perform benzylic hydroxylations with high enantioselectivity is revealed. The substrate repertoire of chloroperoxidase is expanded and the enantioselectivity data for synthetically useful epoxidations are reported. The enzyme epoxidizes straight chain aliphatic and cyclic cis-olefins in a highly stereoselective manner favoring small unsubstituted substrates in which the double bond is not more than two carbon atoms from the terminal. The epoxidation of short-chain prochiral terminal dienes proceeds with high diastereoselectivity and moderate enantioselectivity, yielding monoepoxides exclusively. Unsubstituted straight-chain terminal olefins seven carbons or longer are epoxidized poorly. Aliphatic and aromatic alcohols are efficiently oxidized to aldehydes and acids. The utilization of radical probe substrate trans-2-phenyl-1-methylcyclopropane revealed that the mechanism of chloroperoxidase-catalyzed hydroxylation is incompatible with the existence of a discrete radical intermediate and most likely proceeds via transfer of the oxygen atom from the high valent iron oxo intermediate directly to the substrate.