PH wave-front propagation in the urea-urease reaction
PH wave-front propagation in the urea-urease reaction
The urease-catalyzed hydrolysis of urea displays feedback that results in a switch from acid (pH ∼3) to base (pH ∼9) after a controllable period of time (from 10 to >5000 s). Here we show that the spatially distributed reaction can support pH wave fronts propagating with a speed of the order of 0.1−1 mm min−1. The experimental results were reproduced qualitatively in reaction-diffusion simulations including a Michaelis-Menten expression for the urease reaction with a bell-shaped rate-pH dependence. However, this model fails to predict that at lower enzyme concentrations, the unstirred reaction does not always support fronts when the well-stirred reaction still rapidly switches to high pH.
610-615
Wrobel, Magdalena M
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Bánsági, Tamás
3984187d-60fd-47f2-b6cb-f312dcedadae
Scott, Stephen K
af27ae5b-ff62-43cb-936f-e49ff15c679c
Taylor, Annette F
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Bounds, Chris O
d166a9b1-cd13-459f-904d-78797956a3dd
Carranza, Arturo
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Pojman, John A
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8 August 2012
Wrobel, Magdalena M
7f1c044b-fabd-4abc-ad86-e08647627454
Bánsági, Tamás
3984187d-60fd-47f2-b6cb-f312dcedadae
Scott, Stephen K
af27ae5b-ff62-43cb-936f-e49ff15c679c
Taylor, Annette F
13fcac52-9c5c-4690-a13a-7d24f1249a33
Bounds, Chris O
d166a9b1-cd13-459f-904d-78797956a3dd
Carranza, Arturo
9d516d06-8e37-4d05-8eed-52eaf71eb8a1
Pojman, John A
d4ab5f67-2edf-48a0-bc95-39f7e10b9b52
Wrobel, Magdalena M, Bánsági, Tamás, Scott, Stephen K, Taylor, Annette F, Bounds, Chris O, Carranza, Arturo and Pojman, John A
(2012)
PH wave-front propagation in the urea-urease reaction.
Biophysical Journal, 103 (3), .
(doi:10.1016/j.bpj.2012.06.020).
Abstract
The urease-catalyzed hydrolysis of urea displays feedback that results in a switch from acid (pH ∼3) to base (pH ∼9) after a controllable period of time (from 10 to >5000 s). Here we show that the spatially distributed reaction can support pH wave fronts propagating with a speed of the order of 0.1−1 mm min−1. The experimental results were reproduced qualitatively in reaction-diffusion simulations including a Michaelis-Menten expression for the urease reaction with a bell-shaped rate-pH dependence. However, this model fails to predict that at lower enzyme concentrations, the unstirred reaction does not always support fronts when the well-stirred reaction still rapidly switches to high pH.
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Published date: 8 August 2012
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Local EPrints ID: 499620
URI: http://eprints.soton.ac.uk/id/eprint/499620
ISSN: 0006-3495
PURE UUID: a1d04efd-561a-4b31-ace2-0bfe2bfa147f
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Date deposited: 27 Mar 2025 18:22
Last modified: 16 Oct 2025 17:52
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Author:
Magdalena M Wrobel
Author:
Tamás Bánsági
Author:
Stephen K Scott
Author:
Annette F Taylor
Author:
Chris O Bounds
Author:
Arturo Carranza
Author:
John A Pojman
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