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Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential
Author(s) -
Frank Annika,
Seel Catharina Julia,
Groll Michael,
Gulder Tanja
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600417
Subject(s) - halogenation , chemistry , biocatalysis , reactivity (psychology) , enzyme , yield (engineering) , combinatorial chemistry , organic chemistry , materials science , catalysis , reaction mechanism , medicine , alternative medicine , pathology , metallurgy
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 Acaryochloris marina ( Am VHPO), including its structure determination by X‐ray crystallography. Compared to other VHPOs, the Am 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.