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In chemistry, biochemistry, and pharmacology, a dissociation constant (K D) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions.
K a is variously named a dissociation constant, [3] an acid ionization constant, [2]: 668 an acidity constant [1] or an ionization constant. [2]: 708 It serves as an indicator of the acid strength: stronger acids have a higher K a value (and a lower pK a value).
Stepwise dissociation constants are each defined for the loss of a single proton. The constant for dissociation of the first proton may be denoted as K a1 and the constants for dissociation of successive protons as K a2, etc. Phosphoric acid, H 3 PO 4, is an example of a polyprotic acid as it can lose three protons.
The constants listed here are known values of physical constants expressed in SI units; that is, physical quantities that are generally believed to be universal in nature and thus are independent of the unit system in which they are measured. Many of these are redundant, in the sense that they obey a known relationship with other physical ...
Stability constants defined in this way, are association constants. This can lead to some confusion as pK a values are dissociation constants. In general purpose computer programs it is customary to define all constants as association constants. The relationship between the two types of constant is given in association and dissociation constants.
Acid strength is the tendency of an acid, symbolised by the chemical formula, to dissociate into a proton, +, and an anion, .The dissociation or ionization of a strong acid in solution is effectively complete, except in its most concentrated solutions.
The term bond-dissociation energy is similar to the related notion of bond-dissociation enthalpy (or bond enthalpy), which is sometimes used interchangeably.However, some authors make the distinction that the bond-dissociation energy (D 0) refers to the enthalpy change at 0 K, while the term bond-dissociation enthalpy is used for the enthalpy change at 298 K (unambiguously denoted DH° 298).
The dissociation rate constant is defined using K off. [2] The Michaelis-Menten constant is denoted by K m and is represented by the equation K m = (K off + K cat)/ K on [definition needed]. The rates that the enzyme binds and dissociates from the substrate are represented by K on and K off respectively.