Proton-magnetic-resonance study of copper(I) complexes with peptides containing sulfhydryl and imidazole groups as possible model ligands for copper proteins.

doi:10.1111/J.1432-1033.1977.TB11755.X

Paper

Proton-magnetic-resonance study of copper(I) complexes with peptides containing sulfhydryl and imidazole groups as possible model ligands for copper proteins.

Published Sep 1, 1977 · Y. Sugiura

European journal of biochemistry

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15

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Abstract

The copper(I) complexes of peptides containing sulfhydryl and imidazole groups have been investigated in aqueous solution by proton magnetic resonance (1H NMR). The N-mercaptoacetyl-L-histidine coordinates through the sulfhydryl sulfur and imidazole nitrogen atoms to form the unique 1:1 Cu(I) complex species containing bridged imidazole. The sulfhydryl and imidazole groups are adequate ligands for not only Cu(II) but also Cu(I). The 1H NMR spectra show that the peptide nitrogen group is not involved in complex formation of Cu(I) with N-mercaptoacetyl-L-histidine and 3-mercaptopropionyl-L-histidine. The results have been discussed with respect to the protein ligands for 'blue' copper centers.

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Key takeawayCopper(I) complexes with peptides containing sulfhydryl and imidazole groups show potential as model ligands for copper proteins, with the peptide nitrogen group not involved in complex formation.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Proton-magnetic-resonance study of copper(I) complexes with peptides containing sulfhydryl and imidazole groups as possible model ligands for copper proteins.

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References

Assignment of a ligand in stellacyanin by a pulsed electron paramagnetic resonance method.

Stellacyanin's electron spin echo decay pattern suggests an imidazole is ligated to the copper in this blue protein, as seen in copper(II) bovine serum albumin.

A possible approach to the investigation of the structures of copper proteins: H N.M.R. spectra of azurin.

Copper proteins from Pseudomonas aeruginosa show varying degrees of copper binding, with some histidines being far from the metal and others bound to it.

Spectroscopic studies and a structural model for blue copper centers in proteins.

Blue copper centers in proteins are characterized by low energy bands at 5000 and 10,000 cm-1, suggesting a flattened tetrahedral structure with ligands identified as His-38, Cys-85, His-88, and a deprotonated peptide nitrogen.

Nuclear magnetic resonance studies of the copper binding sites of blue copper proteins: oxidized, reduced, and apoplastocyanin.

Copper binding in plastocyanins stabilizes the protein structure without major reorganization, but does not cause major reorganization of the protein.

The copper coordination group in "blue" copper proteins: evidence from resonance Raman spectra.

The "blue" copper site in proteins like azurin, plastocyanin, and ceruloplasmin exhibits approximately trigonal-bipyramidal coordination, with a sulfur and two nitrogen ligands in the equatorial plane and less strongly bound nitrogen or oxygen

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