Structural Snapshots of a Flexible Cu_2P_2 Core that Accommodates the Oxidation States Cu~ICu~I,Cu~(1.5)Cu~(1.5),and Cu~(II)Cu~(II)

摘要

Understanding how nature controls electron transfer (ET) rates in copper-containing proteins,such as the "blue copper" protein family,has provided impetus for theoretical,biochemical,and small molecule model studies.It is generally accepted that structural reorganization as a function of ET needs to be minimized if rapid rates are to be achieved,and that this cart be difficult to accomplish in synthetic copper systems due to ligand rearrangement,loss,and exchange processes.