A De Novo Designed Metalloprotein Displays Variable Thermal Stability and Binding Stoichiometry with Transition Metal Ions.

ABSTRACT: Metal-binding selectivity in natural proteins is determined by multiple factors such as the protein's structure, metal concentration within cellular compartments, and the presence of metallochaperones. The in vitro selectivity of proteins for transition metal ions is largely governed by the Irving-Williams series, which states protein-metal complex stability follows the order Co(II) < Ni(II) < Cu(II) > Zn(II). A de novo protein has been designed that folds in the presence of certain transition metal ions into a monomeric α-helical bundle, with the least stable protein-metal complex being formed with Cu(II). Moreover, when increasing the metal concentration of Cu(II) or Zn(II), more metal ions are incorporated into the protein accompanied by a concurrent decrease in the amount of secondary

SUBMITTER: Rooijakkers B 

PROVIDER: S-EPMC12278340 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature