Search results

Sort By:

Limit search:

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

100%

Anamaria I., Mot A., Silaghi-Dumitrescu R.

Open Chemistry

2012

vol. 10

issue 5

1527-1533

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. [...]

Refine search results

1 Open Chemistry

1 2012

1 Anamaria I.

1 Mot A.

1 Silaghi-Dumitrescu R.

Search results

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