Exploring the possibility of high-valent copper in models of copper proteins with a three-histidine copper-binding motif

• Authors: Imre Anamaria , Augustin Mot , Radu Silaghi-Dumitrescu
• Languages of publication: EN

Abstracts

EN

An important function of many copper-containing proteins is activation of O2 and subsequent substrate oxidation. The Cu (III) oxidation state is generally considered to be less accessible because of the highly positive Cu (III)/Cu (II) redox potentials with typical amino acid ligands. Here, we employ density functional (DFT) calculations to explore to what extent copper (III) may be accessed in a biologically-relevant coordination environment around a mononuclear copper center, by breaking the oxygen-oxygen bond in a copper-(hydro) peroxide complex. In agreement with previous findings by Solomon and co-workers on copper models with related coordination patterns, the formally high-valent copper complex produced by O-O bond cleavage appears to harbor both oxidizing equivalents on the ligands. The potential energy surface for such a reaction reveals that with the three-histidine binding motif at the copper, O-O bond cleavage is not impossible, but rather disfavored thermodynamically. [...]

Keywords

EN

High-valent copper; Copper proteins; Oxygen-oxygen bond activation; DFT

• Publisher: De Gruyter Open
• Journal: Open Chemistry
• Year: 2012
• Volume: 10
• Issue: 5
• Pages: 1527-1533

Dates

published

1 - 10 - 2012

online

21 - 7 - 2012

Contributors

author

Imre Anamaria

• Department of Chemistry, “Babes-Bolyai University, Cluj-Napoca, RO-400028, Romania

author

Augustin Mot

• Department of Chemistry, “Babes-Bolyai University, Cluj-Napoca, RO-400028, Romania

author

Radu Silaghi-Dumitrescu

• Department of Chemistry, “Babes-Bolyai University, Cluj-Napoca, RO-400028, Romania

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Identifiers

DOI

10.2478/s11532-012-0069-3