A vanadium-51 NMR study of the binding of vanadate and peroxovanadate to proteins.

@article{Rehder2004AVN,
  title={A vanadium-51 NMR study of the binding of vanadate and peroxovanadate to proteins.},
  author={Dieter Rehder and Marian Casn{\'y} and Reiner Grosse},
  journal={Magnetic resonance in chemistry : MRC},
  year={2004},
  volume={42 9},
  pages={745-9}
}
51V quadrupolar central transition NMR spectra of buffered (pH 7.6-8.0) solutions of bovine apo-transferrin (Tf) and bovine prostatic acid phosphatase (Pp) treated with vanadate show normal features (chemical shifts between -515 and -542 ppm) corresponding to the complexation of VO2+ to the Tf binding site and the Pp active centre, respectively. Addition of H2O2 leads to the temporary formation of complexed VO(O2)+ (delta approximately -595). Vanadate-dependent bromoperoxidase from the alga… CONTINUE READING

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