Effect of circular permutation on the structure and function of type 1 blue copper center in azurin.

ABSTRACT: Type 1 copper (T1Cu) proteins are electron transfer (ET) proteins involved in many important biological processes. While the effects of changing primary and secondary coordination spheres in the T1Cu ET function have been extensively studied, few report has explored the effect of the overall protein structural perturbation on active site configuration or reduction potential of the protein, even though the protein scaffold has been proposed to play a critical role in enforcing the entatic or "rack-induced" state for ET functions. We herein report circular permutation of azurin by linking the N- and C-termini and creating new termini in the loops between 1^st and 2^nd β strands or between 3^rd and 4^th β strands. Characterization by electronic absorpti

SUBMITTER: Yu Y 

PROVIDER: S-EPMC5275729 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature