• Media type: E-Article
  • Title: Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential
  • Contributor: Frank, Annika; Seel, Catharina Julia; Groll, Michael; Gulder, Tanja
  • Published: Wiley, 2016
  • Published in: ChemBioChem
  • Extent: 2028-2032
  • Language: English
  • DOI: 10.1002/cbic.201600417
  • ISSN: 1439-4227; 1439-7633
  • Keywords: Organic Chemistry ; Molecular Biology ; Molecular Medicine ; Biochemistry
  • 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>
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