Piwonski 2012 Proc Natl Acad Sci U S A: Difference between revisions
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{{Publication | {{Publication | ||
|title=Piwonski HM, Goomanovsky M, Bensimon D, Horovitz A, Haran G (2012) Allosteric inhibition of individual enzyme molecules trapped in lipid vesicles. Proc Natl Acad Sci | |title=Piwonski HM, Goomanovsky M, Bensimon D, Horovitz A, Haran G (2012) Allosteric inhibition of individual enzyme molecules trapped in lipid vesicles. Proc Natl Acad Sci U S A 109:E1437-43. | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/22562794/ PMID:22562794 Open Access] | |info=[https://pubmed.ncbi.nlm.nih.gov/22562794/ PMID:22562794 Open Access] | ||
|authors=Piwonski HM, Goomanovsky M, Bensimon D, Horovitz A, Haran G | |authors=Piwonski HM, Goomanovsky M, Bensimon D, Horovitz A, Haran G | ||
|year=2012 | |year=2012 | ||
|journal=Proc Natl Acad Sci | |journal=Proc Natl Acad Sci U S A | ||
|abstract=Enzymatic inhibition by product molecules is an important and widespread phenomenon. We describe an approach to study product inhibition at the single-molecule level. Individual HRP molecules are trapped within surface-tethered lipid vesicles, and their reaction with a fluorogenic substrate is probed. While the substrate readily penetrates into the vesicles, the charged product (resorufin) gets trapped and accumulates inside the vesicles. Surprisingly, individual enzyme molecules are found to stall when a few tens of product molecules accumulate. Bulk enzymology experiments verify that the enzyme is noncompetitively inhibited by resorufin. The initial reaction velocity of individual enzyme molecules and the number of product molecules required for their complete inhibition are broadly distributed and dynamically disordered. The two seemingly unrelated parameters, however, are found to be substantially correlated with each other in each enzyme molecule and over long times. These results suggest that, as a way to counter disorder, enzymes have evolved the means to correlate fluctuations at structurally distinct functional sites. | |abstract=Enzymatic inhibition by product molecules is an important and widespread phenomenon. We describe an approach to study product inhibition at the single-molecule level. Individual HRP molecules are trapped within surface-tethered lipid vesicles, and their reaction with a fluorogenic substrate is probed. While the substrate readily penetrates into the vesicles, the charged product (resorufin) gets trapped and accumulates inside the vesicles. Surprisingly, individual enzyme molecules are found to stall when a few tens of product molecules accumulate. Bulk enzymology experiments verify that the enzyme is noncompetitively inhibited by resorufin. The initial reaction velocity of individual enzyme molecules and the number of product molecules required for their complete inhibition are broadly distributed and dynamically disordered. The two seemingly unrelated parameters, however, are found to be substantially correlated with each other in each enzyme molecule and over long times. These results suggest that, as a way to counter disorder, enzymes have evolved the means to correlate fluctuations at structurally distinct functional sites. | ||
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== Cited by == | == Cited by == | ||
{{Template:Cited by | {{Template:Cited by Komlodi 2021 MitoFit AmR-O2}} | ||
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|additional=MitoFit 2021 | |additional=MitoFit 2021 AmR-O2 | ||
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Latest revision as of 21:40, 24 September 2021
| Piwonski HM, Goomanovsky M, Bensimon D, Horovitz A, Haran G (2012) Allosteric inhibition of individual enzyme molecules trapped in lipid vesicles. Proc Natl Acad Sci U S A 109:E1437-43. |
Piwonski HM, Goomanovsky M, Bensimon D, Horovitz A, Haran G (2012) Proc Natl Acad Sci U S A
Abstract: Enzymatic inhibition by product molecules is an important and widespread phenomenon. We describe an approach to study product inhibition at the single-molecule level. Individual HRP molecules are trapped within surface-tethered lipid vesicles, and their reaction with a fluorogenic substrate is probed. While the substrate readily penetrates into the vesicles, the charged product (resorufin) gets trapped and accumulates inside the vesicles. Surprisingly, individual enzyme molecules are found to stall when a few tens of product molecules accumulate. Bulk enzymology experiments verify that the enzyme is noncompetitively inhibited by resorufin. The initial reaction velocity of individual enzyme molecules and the number of product molecules required for their complete inhibition are broadly distributed and dynamically disordered. The two seemingly unrelated parameters, however, are found to be substantially correlated with each other in each enzyme molecule and over long times. These results suggest that, as a way to counter disorder, enzymes have evolved the means to correlate fluctuations at structurally distinct functional sites.
Cited by
- Komlódi T, Sobotka O, Gnaiger E (2021) Facts and artefacts on the oxygen dependence of hydrogen peroxide production using Amplex UltraRed. Bioenerg Commun 2021.4. https://doi:10.26124/BEC:2021-0004
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