Journal
ACS CATALYSIS
Volume 3, Issue 4, Pages 560-564Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cs300766d
Keywords
nanostructures; enzymes; DNA interactions; Sabatier; horseradish peroxidase
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Funding
- Bourns College of Engineering at the University of California, Riverside
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Advances in DNA bionanotechnology have led to the ability to create structures with well-defined chemical and physical features at the nanoscale. Such nanostructures can be used to create spatially organized enzymatic cascades that promote substrate channeling and result in enhanced cascade kinetics. Here, we investigate the effects of substrate-scaffold interactions on the catalytic activity of an enzyme-DNA complex using horseradish peroxidase (HRP) and a nanoscale DNA scaffold with three addressable sites. Kinetic assays with a library of HRP substrates revealed that DNA scaffolding enhances HRP activity in a manner that is analogous to the Sabatier Principle. In this case, the binding of the substrate is to the scaffold and not to the catalyst, but the Sabatier trend holds: weak and strong binding substrates showed no enhancement in kinetics, whereas intermediately bound substrates result in >300% increase in enzyme activity.
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