Engineering a Conformationally Switchable Artificial Metalloprotein.

ABSTRACT: Many naturally occurring metalloenzymes are gated by rate-limiting conformational changes, and there exists a critical interplay between macroscopic structural rearrangements of the protein and subatomic changes affecting the electronic structure of embedded metallocofactors. Despite this connection, most artificial metalloproteins (ArMs) are prepared in structurally rigid protein hosts. To better model the natural mechanisms of metalloprotein reactivity, we have developed conformationally switchable ArMs (swArMs) that undergo a large-scale structural rearrangement upon allosteric effector binding. The swArMs reported here contain a Co(dmgH)₂(X) cofactor (dmgH = dimethylglyoxime and X = N₃^-, H₃C^-, and ⁱPr^-)

SUBMITTER: Fatima S 

PROVIDER: S-EPMC10290874 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature