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Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins

Peisach, J., Blumberg, W.E.·1974·Archives of Biochemistry and Biophysics

Abstract

An extension of a method relating chemical structure to the EPR parameters A∥ and g∥ is presented. For complexes having the same atoms of ligation, a decrease in charge of the metal-ligand complex decreases g∥ and increases A∥. From this analysis, one concludes that in artificial copper proteins as well as in the naturally occurring nonblue copper proteins copper is ligated to oxygen and nitrogen but not to sulfur. A method is presented for the interpretation of EPR changes that occur with ligand exchange reactions at the Type 2 (nonblue) copper sites such as occur in laccase.

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Metadata

Authors
Peisach, J., & Blumberg, W. E.
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
1974-12
Volume
165
Issue
2
Pages
691-708
ISSN
0003-9861 (ISSN-L)
OpenAlex
W1975098194
Cited by
1,354
References
0
FWCI
10.23
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins. https://app.cochat.ai/papers/10.1016/0003-9861(74)90298-7
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Peisach, J., & Blumberg, W. E. (1974). Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins. Archives of Biochemistry and Biophysics. https://doi.org/10.1016/0003-9861(74)90298-7

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.