Atomic differentiation of silver binding preference in protein targets: Escherichia coli malate dehydrogenase as a paradigm.

ABSTRACT: Understanding how metallodrugs interact with their protein targets is of vital importance for uncovering their molecular mode of actions as well as overall pharmacological/toxicological profiles, which in turn facilitates the development of novel metallodrugs. Silver has been used as an antimicrobial agent since antiquity, yet there is limited knowledge about silver-binding proteins. Given the multiple dispersed cysteine residues and histidine-methionine pairs, Escherichia coli malate dehydrogenase (EcMDH) represents an excellent model to investigate silver coordination chemistry as well as its targeting sites in enzymes. We show by systematic biochemical characterizations that silver ions (Ag⁺) bind EcMDH at multiple sites including three cysteine-containin

SUBMITTER: Wang H 

PROVIDER: S-EPMC8162793 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature