Flexible Assembly of an Enzyme Cascade on a DNA Triangle Prism Nanostructure for the Controlled Biomimetic Generation of Nitric Oxide

Zhou, L; Liu, Y; Shi, H; Yang, X; Huang, J; Liu, S; Chen, Q; Liu, J; Wang, K

HERO ID

4943119

Reference Type

Journal Article

Year

2018

Language

English

PMID

29985553

HERO ID 4943119
In Press No
Year 2018
Title Flexible Assembly of an Enzyme Cascade on a DNA Triangle Prism Nanostructure for the Controlled Biomimetic Generation of Nitric Oxide
Authors Zhou, L; Liu, Y; Shi, H; Yang, X; Huang, J; Liu, S; Chen, Q; Liu, J; Wang, K
Journal ChemBiochem
Volume 19
Issue 19
Page Numbers 2099-2106
Abstract Spatial organization of multiple enzymes at specific positions for a controlled reaction cascade has attracted wide attention in recent years. Here, we report the construction of a biomimetic enzyme cascade organized on DNA triangle prism (TP) nanostructures to enable the efficient catalytic production of nitric oxide (NO) on a single microbead. Two enzymes, glucose oxidase (GOx) and horseradish peroxidase (HRP), were assembled at adjacent locations on a DNA TP nanostructure by using DNA-binding protein adaptors with small interenzyme distances. In the cascade, the first enzyme, GOx, converts glucose into gluconic acid in the presence of oxygen. The produced H2 O2 intermediate is rapidly transported to the second enzyme, HRP, which oxides hydroxyurea into NO and other nitroxyl species. The pH near the surface of the negatively charged DNA nanostructures is believed to be lower than that in the bulk solution; this creates an optimal pH environment for the anchored enzymes, which results in higher yields of the NO product. Furthermore, the multienzyme system was immobilized on a microbead mediated by a DNA adaptor, and this enabled the efficient catalytic generation of gas molecules in the microreactor. Therefore, this work provides an alternative route for the biomimetic generation of NO through enzyme cascades. In particular, the dynamic binding capability of the DNA sequence enabled the positions of the protein enzyme and the DNA nanostructure to be reversed, which allowed the cascade catalysis to be modulated.
Doi 10.1002/cbic.201800337
Pmid 29985553
Wosid WOS:000446429400013
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English