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Issue 44, 2019
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Revealing the transient conformations of a single flavin adenine dinucleotide using an aerolysin nanopore

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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 current blockages, the “stack”, “open”, and four quasi-stacked FADs are clearly determined in solution, which is further confirmed by temperature-dependent experiments and mutant aerolysin assay. Combined with molecular dynamics simulations, we achieved a direct correlation between the residual current ratio (I/I0) and FAD backbone angle. These results would facilitate further understanding of the structure–activity relationship in the flavoprotein.

Graphical abstract: Revealing the transient conformations of a single flavin adenine dinucleotide using an aerolysin nanopore

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Supplementary files

Article information


Submitted
27 Jun 2019
Accepted
20 Sep 2019
First published
23 Sep 2019

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2019,10, 10400-10404
Article type
Edge Article

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

M. Li, Y. Wang, Y. Ying and Y. Long, Chem. Sci., 2019, 10, 10400
DOI: 10.1039/C9SC03163D

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