Paramagnetic Properties of the Halide-Bound Derivatives of Oxidised Tyrosinase Investigated by 1H NMR Spectroscopy

The 1H NMR relaxation characteristics of the histidines in the oxidised type‐3 copper site of tyrosinase (Tymet) from the bacterium Streptomyces antibioticus in the halide‐bound forms (TymetX with X = F−, Cl−, Br−) have been determined and analysed. The 1H NMR spectra of the TymetX species display r...

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Veröffentlicht in:	Chemistry : a European journal 2006-10, Vol.12 (29), p.7668-7675
Hauptverfasser:	Tepper, Armand W. J. W., Bubacco, Luigi, Canters, Gerard W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Copper electronic structure enzymes Halogens - chemistry Histidine - chemistry Magnetic Resonance Spectroscopy Magnetics Monophenol Monooxygenase - chemistry NMR spectroscopy relaxation Streptomyces antibioticus Streptomyces antibioticus - enzymology Temperature
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