Unraveling the molecular basis of substrate specificity and halogen activation in vanadium-dependent haloperoxidases.

ABSTRACT: Vanadium-dependent haloperoxidases (VHPOs) are biotechnologically valuable and operationally versatile biocatalysts. VHPOs share remarkable active-site structural similarities yet display variable reactivity and selectivity. The factors dictating substrate specificity and, thus, a general understanding of VHPO reaction control still need to be discovered. This work's strategic single-point mutation in the cyanobacterial bromoperoxidase AmVHPO facilitates a selectivity switch to allow aryl chlorination. This mutation induces loop formation that interacts with the neighboring protein monomer, creating a tunnel to the active sites. Structural analysis of the substrate-R425S-mutant complex reveals a substrate-binding site at the interface of two adjacent units. There, residues Glu139 and Phe40

SUBMITTER: Zeides P 

PROVIDER: S-EPMC11871015 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature