Vanadium metal has been underused in biological applications because of its Lewis acidic properties that make it hydrolysis prone and difficult to work with in water. Possessing a wide range of accessible oxidation states and complex speciation, V has broad applications in industrial catalytic settings, showing that it can be capable of important catalysis, if properly controlled. It may be possible to utilize hydrolysis-prone metals in aqueous chemistry by using naturally occurring protein mechanisms that protect hydrolysis-prone metals from reacting with water as models. The coordination residues in the binding sites of naturally occurring metal binding proteins offer insight for studying how they can prevent hydrolysis and keep the metal soluble in aqueous solution. De novo protein design reduces these naturally-occurring proteins to their active site and structurally required scaffold to enable studies of folding, structure, and function. Due Ferri proteins are de novo designed proteins that have been modified to mimic the binding sites of naturally occurring iron binding proteins and make it possible to investigate the ability of hydrolysis-prone vanadium metal to bind to de novo designed proteins. This study aimed to demonstrate that vanadium can successfully and stably bind to the de novo designed Due Ferri single chain proteins G14D and G14D/I100Y. CD spectroscopic data has demonstrated that V introduce a more organized alpha helical structure to our proteins of interest. Highly suggestive that the proteins are binding the metal, it has never been documented that a de novo protein could consistently and stably bind to vanadium metal. The capacity for a protein to bind vanadium is the first step in unlocking its aqueous catalytic abilities. Further studies are underway to determine the ability of V-bound protein complexes to carry out controlled hydrolytic cleavage of substrates ranging from small molecules to DNA.

Towards new vanadium enzymes

2019 Spring National Meeting

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