Traversing the Red-Green-Blue Color Spectrum in Rationally Designed Cupredoxins.

ABSTRACT: Blue copper proteins have a constrained Cu(II) geometry that has proven difficult to recapitulate outside native cupredoxin folds. Previous work has successfully designed green copper proteins which could be tuned blue using exogenous ligands, but the question of how one can create a self-contained blue copper site within a de novo scaffold, especially one removed from a cupredoxin fold, remained. We have recently reported a red copper protein site within a three helical bundle scaffold which we later revisited and determined to be a nitrosocyanin mimic, with a CuHis₂CysGlu binding site. We now report efforts to rationally design this construct toward either green or blue copper chromophores using mutation strategies that have proven successful in native cupredoxins. By rotating

SUBMITTER: Koebke KJ 

PROVIDER: S-EPMC7484265 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature