Related Experiment Video
Updated: Nov 6, 2025

09:38
Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
Published on: July 1, 2021
1.5K
pH-Sensitive Oscillatory Motion of a Urease Motor on the Urea Aqueous Phase
Yu Xu1, Lin Ji2, Shunsuke Izumi1
1Department of Mathematical and Life Sciences, Graduate School of Integrated Sciences for Life, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima, 739-8526, Japan.
Chemistry, an Asian Journal
|May 6, 2021
Summary
Self-propelled urease motors exhibit pH-dependent motion on urea solutions. The enzyme
Area of Science:
- Biochemistry
- Chemical Engineering
- Materials Science
Background:
- Enzyme-driven self-propulsion is a growing field.
- Urease enzyme catalyzes urea hydrolysis, producing ammonia and carbon dioxide.
- Surface tension gradients can generate motion in micro-objects.
Purpose of the Study:
- Investigate self-propelled motion of a urease motor at the air/aqueous interface.
- Determine the effect of initial pH on motor motion and dynamics.
- Elucidate the mechanisms driving oscillatory and non-oscillatory motion.
Main Methods:
- Fabrication of a urease motor using immobilized urease on filter paper.
- Observation of motor behavior on aqueous urea solutions with varying initial pH.
- Analysis of motion dynamics, including frequency and speed.
- Correlation of motion with urease enzyme activity and surface tension gradients.
Main Results:
- The urease motor demonstrated pH-dependent self-propelled motion.
- Oscillatory motion was observed, with frequency and speed varying with initial pH.
- No motion was observed at certain pH values.
- The observed behaviors were linked to the bell-shaped pH-activity profile of urease and surface tension effects.
Conclusions:
- The pH of the urea solution critically influences the self-propulsion of urease motors.
- Urease enzyme's pH-dependent activity and resulting surface tension gradients are key to motion control.
- This study provides insights into enzyme-powered micro-machines and their environmental responsiveness.
Related Concept Videos
Mechanism of Ciliary Motion
4.3K
The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
4.3K
Chemotaxis in E. coli
322
Chemotaxis in Escherichia coli is a sensory-driven motility mechanism that enables bacteria to navigate chemical gradients, moving toward beneficial environments while avoiding harmful conditions. This process relies on a signal transduction system integrating external chemical cues with flagellar motor control.Chemoreceptors and Signal DetectionE. coli detects chemical gradients through methyl-accepting chemotaxis proteins (MCPs), which are membrane-bound chemoreceptors that sense attractants...
322
ATP Synthase: Structure
13.9K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
13.9K
Urea Cycle
47.6K
The urea cycle describes how liver cells convert ammonia to urea. Ammonia is a toxic waste product of protein catabolism. Land animals must convert ammonia into the less toxic urea which can be safely eliminated by the kidneys through urine. Marine animals excrete ammonia directly, and the surrounding water dilutes the ammonia to safe levels.
47.6K
ATP Driven Pumps II: P-type Pumps
5.5K
The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
5.5K
The Movement of Organelles and Vesicles
5.2K
In eukaryotic cells, cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
5.2K

