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Stoichiometry of the α-complementation reaction of Escherichia coli β-galactosidase as revealed through single-molecule studies.

Authors
  • Mogalisetti, Pratyusha
  • Walt, David R
Type
Published Article
Journal
Biochemistry
Publisher
American Chemical Society
Publication Date
Mar 03, 2015
Volume
54
Issue
8
Pages
1583–1588
Identifiers
DOI: 10.1021/bi5015024
PMID: 25668156
Source
Medline
License
Unknown

Abstract

The α-complementation reaction of β-galactosidase was studied at single-molecule resolution using arrays of femtoliter-sized wells. Single molecules of the complementation species were observed to be stable for long periods of time, demonstrating that the α-complementation reaction is irreversible. By directly counting the number of active molecules formed in the complementation reaction when different concentrations of enzyme acceptor (EA) and enzyme donor (ED) are used, we deduce that the EA:ED ratio in the complementation species is 4:1.

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