ArticleThe journal of physical chemistry. B2014
Single-molecule enzymatic conformational dynamics: spilling out the product molecules.
Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Memory effects of transcription regulator-DNA interactions in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Strong Plasmon Enhancement of the Saturation Photon Count Rate of Single Molecules.The journal of physical chemistry letters · 2020Article
- Recent progress in dissecting molecular recognition by DNA polymerases with non-native substrates.Current opinion in chemical biology · 2017Review
- Real-time monitoring of conformational transitions of single-molecule histone deacetylase 8 with nanocircuits.Chemical communications (Cambridge, England) · 2017Article
- Probing conformational dynamics of an enzymatic active site by an in situ single fluorogenic probe under piconewton force manipulation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Single Molecule Bioelectronics and Their Application to Amplification-Free Measurement of DNA Lengths.Biosensors · 2016Article
- Protein Conformational Landscapes and Catalysis. Influence of Active Site Conformations in the Reaction Catalyzed by L-Lactate Dehydrogenase.ACS catalysis · 2015Article
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Authors and funding
2 authors.
Funding
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Abstract
Product releasing is an essential step of an enzymatic reaction, and a mechanistic understanding primarily depends on the active-site conformational changes and molecular interactions that are involved in this step of the enzymatic reaction. Here we report our work on the enzymatic product releasing dynamics and mechanism of an enzyme, horseradish peroxidase (HRP), using combined single-molecule time-resolved fluorescence intensity, anisotropy, and lifetime measurements. Our results have shown a wide distribution of the multiple conformational states involved in active-site interacting with the product molecules during the product releasing. We have identified that there is a significant pathway in which the product molecules are spilled out from the enzymatic active site, driven by a squeezing effect from a tight active-site conformational state, although the conventional pathway of releasing a product molecule from an open active-site conformational state is still a primary pathway. Our study provides new insight into the enzymatic reaction dynamics and mechanism, and the information is uniquely obtainable from our combined time-resolved single-molecule spectroscopic measurements and analyses.
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