Biochemical and Structural Characterization of XoxG and XoxJ and Their Roles in Lanthanide-Dependent Methanol Dehydrogenase Activity.

ABSTRACT: Lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have recently been shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems contain two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function), about which little is known. In this work, we have biochemically and structurally characterized these proteins from the methyltroph Methylobacterium extorquens AM1. In contrast to results obtained in an artificial assay system, assays of XoxFs metallated with La^III , Ce^III , and Nd^III using their physiological electron acceptor, XoxG, display Ln-independent activities, but the K_m for XoxG markedly increases from La to Nd. This result suggests that XoxG's

SUBMITTER: Featherston ER 

PROVIDER: S-EPMC6814260 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature