1H NMR spectroscopy of the binuclear Cu(II) active site of Streptomyces antibioticus tyrosinase
Open Access
- 15 January 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 442 (2-3) , 215-220
- https://doi.org/10.1016/s0014-5793(98)01662-7
Abstract
The 600 MHz 1H NMR spectrum of tyrosinase (31 kDa) of Streptomyces antibioticus in the oxidized, chloride‐bound form is reported. The downfield part of the spectrum (15–55 ppm) exhibits a large number of paramagnetically shifted signals. The paramagnetism is ascribed to a thermally populated triplet state. The signals derive from six histidines binding to the metals through their Nϵ atoms. There is no evidence for endogenous bridges. The exchange coupling, −2J, amounts to 298 cm−1. In the absence of chloride the peaks broaden. This is ascribed to a slowing down of the electronic relaxation. The exchange coupling decreases to −2J=103 cm−1.Keywords
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