文摘
Stellacyanin from Rhus vernificera is a blue copperprotein in which the metal is coordinatedto a Cys, two His, and a Gln residue. It displays a low redoxpotential, a fast electron exchange rate, anda reversible alkaline transition. We have studied this transitionin Cu(II)- and Co(II)-stellacyanin bymeans of electronic and NMR spectroscopy. The data indicate that aconformational rearrangement ofthe metal site occurs at high pH. A drastic alteration in the Glncoordination mode, as initially proposed,is discarded. These results show that the metal site instellacyanin is more flexible than the sites of otherblue copper proteins. The present study demonstrates that theparamagnetic shifts of the bound Cys inthe Co(II) derivative are sensitive indicators of the electrondelocalization and conformational changesexperienced by this residue.