Electron-transfer rates in proteins containing blue copper centers such as plast

Question

Electron-transfer rates in proteins containing blue copper centers such as plastocyanin can be high, as exemplified by the rate constant of electron self-exchange of 1.3 Times 10^6 M^-1s^-1 for azurin. These sites have relatively small ligand reorganization energies, since the copper geometry of the oxidized and reduced forms is very similar, and this feature has been suggested as one reason why the rates are so high. Recently, CuL_2^n+ complexes, n = 1 or 2, were prepared where L is a bidentate bis(imidazole) ligand. The structures are both tetrahedral with average Cu-N bond lengths of 1.96 A for the Cu(II) form and 2.03 A for the Cu(I) form. Studies of the self-exchange electron-transfer rate for this couple revealed a self-exchange rate constant of

Explanation / Answer

The rates of the CuL2 system is slower than the azurin system by a factor of around 10000.

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