Publications by authors named "Elise J Mostad"
Ceruloplasmin (Cp), a multicopper ferroxidase, is expressed as both a secreted (sCp) plasma enzyme from the liver and a membrane-bound glycosylphosphatidylinositol-anchored (GPI-Cp) splice variant protein. Cp is thought to be essential for iron mobilization as selective iron overload occurs in aceruloplasminemia in humans and in Cp null mice. Dietary copper-deficient (CuD) rodents have near total loss of Cp activity, severe loss of Cp protein and develop anemia.
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- Researchers used loop-directed mutagenesis to swap the copper-binding loop of a blue copper protein called azurin with a loop from a red copper protein named nitrosocyanin, creating a new variant called NC-azurin.
- The newly formed NC-azurin exhibited a red color and showed UV-vis absorption and EPR spectra similar to the nitrosocyanin parent.
- Although adding a fourth copper ligand led to changes in stability and properties that deviated from both parent proteins, the loop replacement alone was sufficient to give NC-azurin the characteristics of a red copper site, with its reduction potential being between the two originals and lower than that of wild-type azurin by 50 mV.