Contrasting synergistic anion effects in vanadium(V) binding to nicatransferrin versus human serum transferrin

Biochemistry. 2009 Dec 15;48(49):11609-11. doi: 10.1021/bi901630j.

Abstract

Some ascidians sequester vanadium and other metal ions that are bound and transported in higher organisms by transferrin. The ascidian Ciona intestinalis has a monolobal transferrin (nicatransferrin) in its plasma. The binding of vanadium(V) to nicatransferrin was investigated by using isothermal titration calorimetry and UV-vis spectroscopy, in the presence and absence of NaHCO(3), and was compared with human serum transferrin. Nicatransferrin and serum transferrin bind V(V) with similar strengths [K = (2.0 +/- 0.6) x 10(5) M(-1) for nicatransferrin]; however, nicatransferrin requires a synergistic anion for V(V) binding, whereas serum transferrin does not. Spectroscopy supports a different kind of coordination site.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Ciona intestinalis / chemistry
  • Ciona intestinalis / metabolism
  • Drug Synergism
  • Humans
  • Protein Binding
  • Protein Transport
  • Sodium Bicarbonate / chemistry
  • Sodium Bicarbonate / metabolism
  • Thermodynamics
  • Transferrin / chemistry*
  • Transferrin / metabolism*
  • Vanadates / chemistry
  • Vanadates / metabolism
  • Vanadium / chemistry*
  • Vanadium / metabolism*

Substances

  • Transferrin
  • Vanadium
  • Vanadates
  • Sodium Bicarbonate
  • ammonium metavanadate