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Pourbaix diagram of iron. [1] The Y axis corresponds to voltage potential. In electrochemistry, and more generally in solution chemistry, a Pourbaix diagram, also known as a potential/pH diagram, E H –pH diagram or a pE/pH diagram, is a plot of possible thermodynamically stable phases (i.e., at chemical equilibrium) of an aqueous electrochemical system.
where ln denotes the natural logarithm, is the thermodynamic equilibrium constant, and R is the ideal gas constant.This equation is exact at any one temperature and all pressures, derived from the requirement that the Gibbs free energy of reaction be stationary in a state of chemical equilibrium.
A typical titration curve of a diprotic acid, oxalic acid, titrated with a strong base, sodium hydroxide.Both equivalence points are visible. Titrations are often recorded on graphs called titration curves, which generally contain the volume of the titrant as the independent variable and the pH of the solution as the dependent variable (because it changes depending on the composition of the ...
[c] [2] For example, a hypothetical weak acid having K a = 10 −5, the value of log K a is the exponent (−5), giving pK a = 5. For acetic acid, K a = 1.8 x 10 −5, so pK a is 4.7. A higher K a corresponds to a stronger acid (an acid that is more dissociated at equilibrium).
Ortho effect is an organic chemistry phenomenon where the presence of a chemical group at the at ortho position or the 1 and 2 position of a phenyl ring, relative to the carboxylic compound changes the chemical properties of the compound.
Such a statement is incorrect. For example, acetic acid is a weak acid which has a = 1.75 x 10 −5. Its conjugate base is the acetate ion with K b = 10 −14 /K a = 5.7 x 10 −10 (from the relationship K a × K b = 10 −14), which certainly does not correspond to a strong base
For example, the acid may be acetic acid and the salt may be sodium acetate. The Henderson–Hasselbalch equation relates the pH of a solution containing a mixture of the two components to the acid dissociation constant, K a of the acid, and the concentrations of the species in solution. [6]
The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...