Copper oxygen binding

Solomon El, Chen P, Metz M, Lee SK, Palmer AE. 2001. Oxygen binding, activation, and reduction to water by copper proteins. Angew Chem Int Ed 40 4570-4590. 

It therefore appears that for at least domains 4 and 6, hCP possesses metal binding sites in addition to the six integral copper atoms. Binding of ferrous iron at these sites could result in its oxidation and its removal from the plasma or in the reduction of oxygen-based free radicals. Binding of copper could result in its transport through the plasma (vide infra). 

In one case pulse-radiolysis techniques were employed to study the effect of pressure on such reactions. The oxidation of [Cu lphenhl by dioxygen proceeds via a Cu1—02 transient in which a copper—oxygen bond is formed, followed by the rapid formation of [Cun(phen)2] and 02 (110). This process is characterized by a AV of 22 cm3 mol1, which is close to the reaction volume expected for the binding of dioxygen. 

Sprakel, V.S.I., Feiters, M.C., Meyer-Klaucke, W., Klopstra, M., Brinksma, J., Feringa, B.L., Karlin, K.D. and Nolte, R.J.M. (2005) Oxygen binding and activation by the complexes of PY2- and TPA-appended diphenylglycoluril receptors with copper and other metals. Dalton Trans., 3522-3534. 

Copper(II) binds some 10-fold more strongly to cephalosporins than to penicillins.411,414 Molecular models indicate that one of the conformations of cephalosporins would be very suitable for binding via the carboxylate group and the /8-lactam carbonyl oxygen (124) giving rise to a seven-membered chelate ring. Variations in the /3-lactam carbonyl stretching frequency on com-plexation provide some support for structure (124). 

He s are very large oxygen-binding copper proteins freely dissolved in the hemolymph of many invertebrates of the two phyla of Arthropoda and Mollusca. Hemocyanin accounts for up to 80-98% of the total protein in the hemolymph. A more detailed description of the distribution of He s in Arthropoda and Mollusca can be found in reviews. ... 

The results suggest that the copper at the oxygen-binding site is at least partly Cu(ii) but no Cu(ii) ESR signal has been detected. (728)... 

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