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Related Concept Videos

Common Ion Effect03:24

Common Ion Effect

41.7K
Compared with pure water, the solubility of an ionic compound is less in aqueous solutions containing a common ion (one also produced by dissolution of the ionic compound). This is an example of a phenomenon known as the common ion effect, which is a consequence of the law of mass action that may be explained using Le Châtelier’s principle. Consider the dissolution of silver iodide:
41.7K
Ionic Strength: Effects on Chemical Equilibria01:19

Ionic Strength: Effects on Chemical Equilibria

1.5K
The addition of an inert ionic compound increases the solubility of a sparingly soluble salt. For example, adding potassium nitrate to a saturated solution of calcium sulfate significantly enhances the solubility of calcium sulfate. Le Châtelier's principle cannot predict this shift in the equilibrium. Instead, this could be explained in terms of changes in the effective concentration of the ions in solution in the presence of added inert salt.
In this solution, the primary...
1.5K
Titration of a Weak Base with a Strong Acid01:20

Titration of a Weak Base with a Strong Acid

5.2K
The titration curve of a weak base like ammonia with a strong acid like hydrochloric acid is the mirror image of the titration curve of a weak acid with a strong base.
Using the ICE table and substituting the Kb value, we calculate the initial pH of 50 mL of 0.1 M ammonia to be 11.11. Addition of 25 mL of 0.1 M hydrochloric acid to this solution of ammonia results in a buffer with an equal concentration of ammonia and ammonium ions. The pH of this buffer can be calculated by substituting these...
5.2K
Solvating Effects02:12

Solvating Effects

7.5K
An understanding of the solvating effect helps rationalize the relation between solvation and acidity of the compound. In addition, this also explains the relative stability of conjugate bases for compounds with different pKa values. This lesson details, in-depth, the principle of solvating effects. The strength of an acid and the stability of its corresponding conjugate base are determined using pKa values. This observed relationship is a consequence of solvation, which is the interaction...
7.5K
Basicity of Aliphatic Amines01:21

Basicity of Aliphatic Amines

5.9K
Amines can behave as Brønsted–Lowry bases by accepting a proton from the acid to form corresponding conjugate acids. Due to a lone pair of nonbonding electrons, aliphatic amines can also act as Lewis bases by forming a covalent bond with an electrophile.
To measure the basicity of amines, two conventions are generally used. The first defines Kb as the basicity constant for the deprotonation reaction of water by the amine, as presented in Figure 1. Conventionally, lower Kb indicates...
5.9K
Relative Strengths of Conjugate Acid-Base Pairs02:29

Relative Strengths of Conjugate Acid-Base Pairs

45.8K
Brønsted-Lowry acid-base chemistry is the transfer of protons; thus, logic suggests a relation between the relative strengths of conjugate acid-base pairs. The strength of an acid or base is quantified in its ionization constant, Ka or Kb, which represents the extent of the acid or base ionization reaction. For the conjugate acid-base pair HA / A−, the ionization equilibrium equations and ionization constant expressions are
45.8K

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Updated: Jul 2, 2025

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Specific anion effects on urease activity: A Hofmeister study.

Mert Acar1, Duccio Tatini1, Marcello A Budroni2

  • 1Department of Chemistry "Ugo Schiff" and CSGI, University of Florence, Sesto Fiorentino, Firenze 50019, Italy.

Colloids and Surfaces. B, Biointerfaces
|February 17, 2024
PubMed
Summary

Urease enzyme activity is modulated by electrolytes. Mild electrolytes are tolerated, but strong kosmotropic and chaotropic anions inhibit urease, offering insights into enzyme mechanisms and potential therapies.

Keywords:
ChaotropicityEnzymatic activityHofmeister seriesKosmotropicityUrease

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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
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Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1
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Area of Science:

  • Biochemistry
  • Enzymology
  • Chemical Kinetics

Background:

  • Urease is a key enzyme involved in urea hydrolysis.
  • Understanding urease activity is crucial for various applications, including medical therapies.
  • Electrolyte interactions with enzymes can significantly alter their function.

Purpose of the Study:

  • To investigate the impact of various electrolytes on urease-catalyzed urea hydrolysis.
  • To analyze the autocatalytic behavior and pH clock reactions of urease.
  • To elucidate the role of specific ion-enzyme interactions and hydration in modulating urease activity.

Main Methods:

  • Enzyme kinetics studies of urea hydrolysis in the presence of diverse electrolytes.
  • Analysis of autocatalysis and pH clock phenomena in unbuffered urease solutions.
  • Concentration-dependent analysis of experimental variables to understand ion effects.

Main Results:

  • Urease exhibits tolerance to mild electrolytes.
  • Strong kosmotropic and chaotropic anions significantly inhibit urease activity.
  • Specific ion-enzyme interactions and hydration effects were identified.

Conclusions:

  • Electrolyte composition critically influences urease function.
  • Findings provide molecular insights into urease-electrolyte interactions.
  • Potential applications include alternative therapies for Helicobacter pylori infections and biomaterial design.