Revealing the transient conformations of a single flavin adenine dinucleotide using an aerolysin nanopore.

ABSTRACT: Flavin adenine dinucleotide (FAD) as a cofactor is involved in numerous important metabolic pathways where the biological function is intrinsically related to its transient conformations. The confined space of enzymes requires FAD set in its specific intermediate conformation. However, conventional methods only detect stable conformations of FAD molecules, while transient intermediates are hidden in ensemble measurements. There still exists a challenge to uncover the transient conformation of each FAD molecule, which hinders the understanding of the structure-activity relationship of the FAD mechanism. Here, we employ the electrochemically confined space of an aerolysin nanopore to directly characterize a series of transient conformations of every individual FAD. Based on distinguishable c

SUBMITTER: Li MY 

PROVIDER: S-EPMC6988595 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature