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. 1977 Aug;74(8):3114–3118. doi: 10.1073/pnas.74.8.3114

Blue copper proteins: Synthesis, spectra, and structures of CuIN3(SR) and CuIIN3(SR) active site analogues

Jeffery S Thompson 1, Tobin J Marks 1, James A Ibers 1
PMCID: PMC431457  PMID: 16592426

Abstract

The reaction of Cu(SR) or [Cu(SR)][ClO4] derivatives (SR = p-nitrobenzenethiolate or O-ethylcysteinate) with potassium hydrotris(3,5-dimethyl-1-pyrazolyl)borate produces redox pairs of the stoichiometry CuIN3(SR) and CuIIN3(SR). These complexes are well-defined synthetic approximations to the proposed N3S binding sites of blue (type 1) copper electron transfer proteins. The compounds were investigated by a variety of chemical and spectral (optical, resonance Raman, and electron paramagnetic resonance) techniques; the complex K[Cu(hydrotris(3,5-dimethyl-1-pyrazolyl)borate)(p- NO2C6H4S]-2 acetone was also studied by single-crystal x-ray diffraction methods. The spectrochemical characteristics of the CuIIN3(SR) species are in large part similar to the native system and thus provide some perspective regarding the origin of the unique type 1 spectral parameters and electron transfer properties.

Keywords: type 1 copper proteins, N3S coordination, charge transfer transitions, resonance Raman spectra, electron paramagnetic resonance spectra

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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