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Peroxovanadates and Its Bio-Mimicking Relation with Vanadium Haloperoxidases
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Author(s): Pranjal Saikia (Gauhati University (IST), India), Saitanya Kumar Bharadwaj (Pragjyotish College, India)and Abu Taleb Miah (Gauhati University (IST), India)
Copyright: 2016
Pages: 23
Source title:
Emerging Research on Bioinspired Materials Engineering
Source Author(s)/Editor(s): Mohamed Bououdina (University of Bahrain, Bahrain)
DOI: 10.4018/978-1-4666-9811-6.ch007
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Abstract
Vanadium Haloperoxidases (VHPOs) have been used in a variety of biotransformations showing remarkable stereoselectivity and regiospecificity. The high efficiency of the enzyme is influenced by the protein active site and the role of certain amino acids in activation of vanadium(V)-bound peroxide for halide oxidation. The use of natural or recombinant enzymes, or biomimetic vanadium compounds brings up issues regarding the cost of production and reaction conditions. In this chapter, the primary intent is to provide a simple and clear picture of functional mimicking nature of peroxovanadium compounds with haloperoxidases enzymes to the readers. Major emphasis would be given to examine the reactivity of the vanadium haloperoxidases with mechanism.
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