Dissociation of Biological Catch-Bond by Periodic Perturbation

Pereverzev, Yuriy V.; Prezhdo, Oleg V.

doi:10.1529/biophysj.106.087288

Cited by 20 publications

(29 citation statements)

References 10 publications

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“…At smaller forces, the Bell term is not able to suppress the deformation term, Eq. (19), responsible for the catchbehavior. This factor contributes to the large catchefficiency of the Human Trx system, sðf m Þ=sð0Þ % 60; Eq.…”

Section: Discussion Of the Experimental Datamentioning

confidence: 99%

“…This bond deformation effect saturates at some force, Eq. (19). Second, the barrier leading to the transition state of the S N 2 reaction is lowered by the force according to the traditional Bell expression, Eq.…”

Section: Discussionmentioning

confidence: 99%

“…The two contributions to the energy barrier separating states 0 and 1, Eqs. (19) and (20), emphasize the fact that the force dependence of the barrier is determined by two independent parameters-the bond/grove alignment angle and the displacement of the sulfur atoms with respect to each other. Combining Eqs.…”

Section: Deformation Model Of Enzyme Catalysis In the Presence Of Forcementioning

confidence: 99%

“…Combining Eqs. (19) and (20), the overall dependence of the reaction rate constant of the applied force can be written in the form…”

Section: Deformation Model Of Enzyme Catalysis In the Presence Of Forcementioning

confidence: 99%

“…The two-pathway model with one bound state is the simplest model of the catch-slip and other 13 phenomena, and its straightforward mathematics leads to many useful analytic results. 19,20,23 One of the conceptual problems with the two-pathway model is the need for two distinct dissociation pathways that must point in opposite directions. It may be hard to visualize the two pathways, especially for such a simple bond as the disulfide.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Deformation Model for Thioredoxin Catalysis of Disulfide Bond Dissociation by Force

Pereverzev

Prezhdo

2009

Cel. Mol. Bioeng.

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Abstract-We develop a theoretical model describing the effect of applied force on the rate of enzymatic dissociation of disulfide bonds (Wiita, A. P. et al., Nature 450:124-127, 2007). The timescale characterizing the extension of the 8-domain protein chain, in which every domain contains a disulfide bond, exhibits anomalous force dependence: The extension time first increases and then decreases with increasing force. This type of force dependence indicates catch-binding and is under active investigation in a variety of systems. The disulfide system presents the first example of a chemical catch-bond. The key difference between the deformation model developed here and the two-pathway model used in the original publication is the bond-deformation term in the force dependence of the dissociation rate constant. The bond-deformation concept provides a different interpretation of the phenomenon. Rather than invoking a new dissociation pathway, which is difficult to rationalize for a simple S-S bond, catch-binding is explained by a force-induced deformation in the protein system disfavoring bond dissociation by thioredoxin. The analysis of the experimental data is performed within the Michaelis-Menten kinetic mechanism of enzyme catalysis. A simplified version of the MichaelisMenten mechanism containing only four parameters is found to provide a quantitative description of the key features of the experimental data.

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Section: Discussion Of the Experimental Datamentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Deformation Model Of Enzyme Catalysis In the Presence Of Forcementioning

confidence: 99%

“…Combining Eqs. (19) and (20), the overall dependence of the reaction rate constant of the applied force can be written in the form…”

Section: Deformation Model Of Enzyme Catalysis In the Presence Of Forcementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Deformation Model for Thioredoxin Catalysis of Disulfide Bond Dissociation by Force

Pereverzev

Prezhdo

2009

Cel. Mol. Bioeng.

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References

2010

Enzyme Kinetics: Catalysis &Amp; Control

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The Two-Pathway Model of the Biological Catch-Bond as a Limit of the Allosteric Model

Pereverzev

Prezhdo

Sokurenko

2011

Biophysical Journal

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Catch-binding is a counterintuitive phenomenon in which the lifetime of a receptor/ligand bond increases when a force is applied to break the bond. Several mechanisms have been proposed to rationalize catch-binding. In the two-pathway model, the force drives the system away from its native dissociation pathway into an alternative pathway involving a higher energy barrier. Here, we analyze an allosteric model suggesting that a force applied to the complex alters the distribution of receptor conformations, and as a result, induces changes in the ligand-binding site. The model assumes explicitly that the allosteric transitions govern the properties of the ligand site. We demonstrate that the dynamics of the ligand is described by two relaxation times, one of which arises from the allosteric site. Therefore, we argue that one can characterize the allosteric transitions by studying the receptor/ligand binding. We show that the allosteric description reduces to the two-pathway model in the limit when the allosteric transitions are faster than the bond dissociation. The formal results are illustrated with two systems, P-selectin/PSGL-1 and FimH/mannose, subjected to both constant and time-dependent forces. The report advances our understanding of catch-binding by combining alternative physical models into a unified description and makes the problem more tractable for the bond mechanics community.

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Dissociation of Biological Catch-Bond by Periodic Perturbation

Cited by 20 publications

References 10 publications

Deformation Model for Thioredoxin Catalysis of Disulfide Bond Dissociation by Force

Deformation Model for Thioredoxin Catalysis of Disulfide Bond Dissociation by Force

References

The Two-Pathway Model of the Biological Catch-Bond as a Limit of the Allosteric Model

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