Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential. (22nd September 2016)

• Record Type: Journal Article
• Authors: Frank, Annika; Seel, Catharina Julia; Groll, Michael; Gulder, Tanja
• Is Part Of: Chembiochem. Volume 17:Number 21(2016)
• Page Start: 2028
• Page End: 2032
• Publication Date: 2016-09-22
• Subjects: enzyme catalysis -- halogenation -- peroxidases -- protein structures -- vanadium; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201600417
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: 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. Abstract : A handy haloperoxidase : The structural and functional characterization of a cyanobacterial vanadium‐dependent haloperoxidase is reported. Easy access by recombinant expression, robustness to organic reaction conditions, and a distinct bromination reactivity make this enzyme a promising tool for biocatalytic halogenations.