Preferential Binding of Lanthanides to Methanol Dehydrogenase Evaluated with Density Functional Theory.

ABSTRACT: Methanol dehydrogenase (MDH) is an enzyme used by certain bacteria for the oxidation of methanol to formaldehyde, which is a necessary metabolic reaction. The discovery of a lanthanide-dependent MDH reveals that lanthanide ions (Ln³⁺) have a role in biology. Two types of MDH exist in methane-utilizing bacteria: one that is Ca²⁺-dependent (MxaF) and another that is Ln³⁺-dependent. Given that the triply charged Ln³⁺ are strongly hydrated, it is not clear how preference for Ln³⁺ is manifested and if the Ca²⁺-dependent MxaF protein can also bind Ln³⁺ ions. A computational approach was used to estimate the Gibbs energy differences between the binding of Ln³⁺ and Ca²⁺ to MDH using den

SUBMITTER: Friedman R 

PROVIDER: S-EPMC8028316 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature