ReviewThe Journal of biological chemistry2010
Single-molecule force spectroscopy approach to enzyme catalysis.
Review in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 77 citations in OpenAlex.
- multiSMD - A Python Toolset for Multidirectional Steered Molecular Dynamics.Journal of chemical information and modeling · 2025Article
- Article
- AFM for Studying the Functional Activity of Enzymes.Biomolecules · 2025Review
- Development of Single Molecule Techniques for Sensing and Manipulation of CRISPR and Polymerase Enzymes.Small (Weinheim an der Bergstrasse, Germany) · 2023Review
- Nanomechanical Study of Enzyme: Coenzyme Complexes: Bipartite Sites in Plastidic Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022Article
- Protein folding modulates the chemical reactivity of a Gram-positive adhesin.Nature chemistry · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Single-molecule theory of enzymatic inhibition.Nature communications · 2018Article
- Chemical kinetics study through observation of individual reaction events with atomic-resolution electron microscopy.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018Review
- A simple DNA handle attachment method for single molecule mechanical manipulation experiments.Protein science : a publication of the Protein Society · 2016Article
- Role of substrate unbinding in Michaelis-Menten enzymatic reactions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Conformational plasticity of the essential membrane-associated mannosyltransferase PimA from mycobacteria.The Journal of biological chemistry · 2013Article
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase.Chemical reviews · 2011Review
- Direct quantification of the attempt frequency determining the mechanical unfolding of ubiquitin protein.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Enzyme catalysis has been traditionally studied using a diverse set of techniques such as bulk biochemistry, x-ray crystallography, and NMR. Recently, single-molecule force spectroscopy by atomic force microscopy has been used as a new tool to study the catalytic properties of an enzyme. In this approach, a mechanical force ranging up to hundreds of piconewtons is applied to the substrate of an enzymatic reaction, altering the conformational energy of the substrate-enzyme interactions during catalysis. From these measurements, the force dependence of an enzymatic reaction can be determined. The force dependence provides valuable new information about the dynamics of enzyme catalysis with sub-angstrom resolution, a feat unmatched by any other current technique. To date, single-molecule force spectroscopy has been applied to gain insight into the reduction of disulfide bonds by different enzymes of the thioredoxin family. This minireview aims to present a perspective on this new approach to study enzyme catalysis and to summarize the results that have already been obtained from it. Finally, the specific requirements that must be fulfilled to apply this new methodology to any other enzyme will be discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.