Abstract:
<jats:title>Abstract</jats:title><jats:p>Vanadium‐dependent haloperoxidases (VHPOs) are a class of halogenating enzymes found in fungi, lichen, algae, and bacteria. We report the cloning, purification, and characterization of a functional VHPO from the cyanobacterium <jats:italic>Acaryochloris marina</jats:italic> (<jats:italic>Am</jats:italic>VHPO), including its structure determination by X‐ray crystallography. Compared to other VHPOs, the <jats:italic>Am</jats:italic>VHPO features a unique set of disulfide bonds that stabilize the dodecameric assembly of the protein. Easy access by high‐yield recombinant expression, as well as resistance towards organic solvents and temperature, together with a distinct halogenation reactivity, make this enzyme a promising starting point for the development of biocatalytic transformations.</jats:p>
Description:
<jats:title>Abstract</jats:title><jats:p>Vanadium‐dependent haloperoxidases (VHPOs) are a class of halogenating enzymes found in fungi, lichen, algae, and bacteria. We report the cloning, purification, and characterization of a functional VHPO from the cyanobacterium <jats:italic>Acaryochloris marina</jats:italic> (<jats:italic>Am</jats:italic>VHPO), including its structure determination by X‐ray crystallography. Compared to other VHPOs, the <jats:italic>Am</jats:italic>VHPO features a unique set of disulfide bonds that stabilize the dodecameric assembly of the protein. Easy access by high‐yield recombinant expression, as well as resistance towards organic solvents and temperature, together with a distinct halogenation reactivity, make this enzyme a promising starting point for the development of biocatalytic transformations.</jats:p>