Ontology highlight
ABSTRACT:
SUBMITTER: Hwang W
PROVIDER: S-EPMC6199318 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature
Nature communications 20181023 1
Metal ions at the active site of an enzyme act as cofactors, and their dynamic fluctuations can potentially influence enzyme activity. Here, we use λ-exonuclease as a model enzyme with two Mg<sup>2+</sup> binding sites and probe activity at various concentrations of magnesium by single-molecule-FRET. We find that while Mg<sub>A</sub><sup>2+</sup> and Mg<sub>B</sub><sup>2+</sup> have similar binding constants, the dissociation rate of Mg<sub>A</sub><sup>2+</sup> is two order of magnitude lower th ...[more]