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Nanoscale Catalyst Chemotaxis Can Drive the Assembly of Functional Pathways
[Image: see text] Recent experiments demonstrate molecular chemotaxis or altered diffusion rates of enzymes in the presence of their own substrates. We show here an important implication, namely, that if a nanoscale catalyst A produces a small-molecule ligand product L which is the substrate of anot...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8366527/ https://www.ncbi.nlm.nih.gov/pubmed/34324352 http://dx.doi.org/10.1021/acs.jpcb.1c04498 |
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author | Kocher, Charles Agozzino, Luca Dill, Ken |
author_facet | Kocher, Charles Agozzino, Luca Dill, Ken |
author_sort | Kocher, Charles |
collection | PubMed |
description | [Image: see text] Recent experiments demonstrate molecular chemotaxis or altered diffusion rates of enzymes in the presence of their own substrates. We show here an important implication, namely, that if a nanoscale catalyst A produces a small-molecule ligand product L which is the substrate of another catalyst B, the two catalysts will attract each other. We explore this nonequilibrium producer recruitment force (ProRec) in a reaction–diffusion model. The predicted cat–cat association will be the strongest when A is a fast producer of L and B is a tight binder to it. ProRec is a force that could drive a mechanism (the catpath mechanism) by which catalysts could become spatially localized into functional pathways, such as in the biochemical networks in cells, which can achieve complex goals. |
format | Online Article Text |
id | pubmed-8366527 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-83665272022-07-29 Nanoscale Catalyst Chemotaxis Can Drive the Assembly of Functional Pathways Kocher, Charles Agozzino, Luca Dill, Ken J Phys Chem B [Image: see text] Recent experiments demonstrate molecular chemotaxis or altered diffusion rates of enzymes in the presence of their own substrates. We show here an important implication, namely, that if a nanoscale catalyst A produces a small-molecule ligand product L which is the substrate of another catalyst B, the two catalysts will attract each other. We explore this nonequilibrium producer recruitment force (ProRec) in a reaction–diffusion model. The predicted cat–cat association will be the strongest when A is a fast producer of L and B is a tight binder to it. ProRec is a force that could drive a mechanism (the catpath mechanism) by which catalysts could become spatially localized into functional pathways, such as in the biochemical networks in cells, which can achieve complex goals. American Chemical Society 2021-07-29 2021-08-12 /pmc/articles/PMC8366527/ /pubmed/34324352 http://dx.doi.org/10.1021/acs.jpcb.1c04498 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Kocher, Charles Agozzino, Luca Dill, Ken Nanoscale Catalyst Chemotaxis Can Drive the Assembly of Functional Pathways |
title | Nanoscale Catalyst Chemotaxis Can Drive the Assembly of Functional
Pathways |
title_full | Nanoscale Catalyst Chemotaxis Can Drive the Assembly of Functional
Pathways |
title_fullStr | Nanoscale Catalyst Chemotaxis Can Drive the Assembly of Functional
Pathways |
title_full_unstemmed | Nanoscale Catalyst Chemotaxis Can Drive the Assembly of Functional
Pathways |
title_short | Nanoscale Catalyst Chemotaxis Can Drive the Assembly of Functional
Pathways |
title_sort | nanoscale catalyst chemotaxis can drive the assembly of functional
pathways |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8366527/ https://www.ncbi.nlm.nih.gov/pubmed/34324352 http://dx.doi.org/10.1021/acs.jpcb.1c04498 |
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