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• W3048322608 endingPage "15294" @default.
• W3048322608 startingPage "15282" @default.
• W3048322608 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 the metal binding site, we created a de novo green copper protein. This in turn was converted to a blue copper protein by removing an axial methionine. Following this rational sequence, we have successfully created red, green, and blue copper proteins within an alpha helical fold, enabling comparisons for the first time of their structure and function disconnected from the overall cupredoxin fold." @default.
• W3048322608 created "2020-08-13" @default.
• W3048322608 creator A5011061327 @default.
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• W3048322608 creator A5084987684 @default.
• W3048322608 date "2020-08-07" @default.
• W3048322608 modified "2023-10-17" @default.
• W3048322608 title "Traversing the Red–Green–Blue Color Spectrum in Rationally Designed Cupredoxins" @default.
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• W3048322608 doi "https://doi.org/10.1021/jacs.0c04757" @default.
• W3048322608 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7484265" @default.
• W3048322608 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32786767" @default.
• W3048322608 hasPublicationYear "2020" @default.
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