A virus-based single-enzyme nanoreactor View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2007-09-23

AUTHORS

Marta Comellas-Aragonès, Hans Engelkamp, Victor I. Claessen, Nico A. J. M. Sommerdijk, Alan E. Rowan, Peter C. M. Christianen, Jan C. Maan, Benedictus J. M. Verduin, Jeroen J. L. M. Cornelissen, Roeland J. M. Nolte

ABSTRACT

Most enzyme studies are carried out in bulk aqueous solution, at the so-called ensemble level, but more recently studies have appeared in which enzyme activity is measured at the level of a single molecule, revealing previously unseen properties1,2,3,4. To this end, enzymes have been chemically or physically anchored to a surface, which is often disadvantageous because it may lead to denaturation. In a natural environment, enzymes are present in a confined reaction space, which inspired us to develop a generic method to carry out single-enzyme experiments in the restricted spatial environment of a virus capsid. We report here the incorporation of individual horseradish peroxidase enzymes in the inner cavity of a virus, and describe single-molecule studies on their enzymatic behaviour. These show that the virus capsid is permeable for substrate and product and that this permeability can be altered by changing pH. More... »

PAGES

635-639

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nnano.2007.299

DOI

http://dx.doi.org/10.1038/nnano.2007.299

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1040165987

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/18654389


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