A vanadium-51 NMR study of the binding of vanadate and peroxovanadate to proteins.
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 Ascophyllum nodosum exhibits an unusually high shielding both for the native (delta = -931) and the peroxo form (delta = -1135) of the enzyme. A resonance at -471 ppm is traced back to an inactive form with oxovanadium(V) in a trigonal-bipyramidal array.
Institut für Anorganische und Angewandte Chemie, Universität Hamburg, 20146 Hamburg, Germany. dieter.rehder@chemie.uni-hamburg.de
Dieter
D
Rehder
Marian
M
Casný
Reiner
R
Grosse
D000135:Acid Phosphatase; D000818:Animals; D001059:Apoproteins / Q000032:analysis / Q000737:chemistry*; D001665:Binding Sites; D002417:Cattle; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D011485:Protein Binding; D017027:Protein Tyrosine Phosphatases / Q000032:analysis / Q000737:chemistry*; D014168:Transferrin / Q000032:analysis / Q000737:chemistry*; D014638:Vanadates / Q000032:analysis / Q000737:chemistry*; D014639:Vanadium
D001059:Apoproteins; D014168:Transferrin; C028284:apotransferrin; C069276:peroxovanadate; D014639:Vanadium; D014638:Vanadates; D000135:Acid Phosphatase; C428439:prostatic acid phosphatase; D017027:Protein Tyrosine Phosphatases