Enzyme Interactions with Labile Oxovanadates and Other Polyoxometalates

  • Crans D
  • 8


    Mendeley users who have this article in their library.
  • 90


    Citations of this article.


Aqueous solutions of vanadate contain several labile oxovanadates; each interacts differently with enzymes and other proteins. Vanadate monomer, V-1, can act as a ground state or transition state analog of phosphate. Vanadate dimer, V-2, inhibits a series of enzymes including dehydrogenases, one aldolase and a phosphatase. V-2 can also activate enzymes, and this activation has been observed with a mutase and dehydrogenase. Vanadate tetramer; V-4 (often referred to as ''metavanadate''), inhibits a large number of enzymes including dehydrogenases, isomerases, and one aldolase. V-4 also binds to a series of enzymes including superoxide dismutase, myosin and possibly adenylate kinase. V-4 has been identified as the species responsible for the specific UV-light induced photocleavage of the active site of myosin and possibly adenylate kinase. Redox chemistry between V-1 and V-4 and proteins has been reported. Vanadate pentamer, V-5, has not yet shown high affinity for proteins, and studies with related oxomolybdates show that a tetramer interacts more potently with the proteins than the pentamer. Vanadate decamer, V-10, is a less labile oxometalate that also inhibits and binds to proteins. The potent antiviral and anti-HIV activity of several oxometalates have increased the interest in protein interactions with large polyoxoanions. It is reasonable to expect that proteins catalyzing reactions of large anionic substrates (polymeric nucleic acids) tend to show high affinity for large polyoxometalates. The fact that other proteins, including cytochrome c, phosphorylase, phosphatases, dehydrogenases and an aldolase, also show affinity for these large polyoxometalates is perhaps more intriguing: this affinity suggests that some sequences and three dimensional arrays might favor binding of oxometalates.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free