A vanadium-51 NMR study of the binding of vanadate and peroxovanadate to proteins |
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Authors: | Rehder Dieter Casný Marian Grosse Reiner |
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Affiliation: | Institut für Anorganische und Angewandte Chemie, Universit?t Hamburg, 20146 Hamburg, Germany. dieter.rehder@chemie.uni-hamburg.de |
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Abstract: | 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. |
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