K ions

In the case of an ionized resin, initially in the H-form and in contact with a solution containing K+ ions, an equilibrium exists ... 

Na[Sb(OH)g], respectively. The latter compound is one of the least soluble sodium salts known and is useful in sodium analysis. Numerous polyantimonate(V) derivatives are prepared by heat treatment of mixtures of antimony trioxide and other metal oxides or carbonates. Of these, K Sb O [12056-59-6] and K Sb O [52015-49-3] have been characterized by x-ray. These consist of three-dimensional networks of SbO in which corners and edges are shared with K" ions located in tunnels through the network (23). Simple species such as SbO and Sb20 2, analogous to orthophosphate and pyrophosphate, apparendy do not exist. 

Figure 12.11 Schematic diagram of the ion pore of the K+ channel. From the cytosolic side the pore begins as a water-filled channel that opens up into a water-filled cavity near the middle of the membrane. A narrow passage, the selectivity filter, links this cavity to the external solution. Three potassium ions (purple spheres) bind in the pore. The pore helices (red) are oriented such that their carboxyl end (with a negative dipole moment) is oriented towards the center of the cavity to provide a compensating dipole charge to the K ions. (Adapted from D.A. Doyle et al.. Science 280 69-77, 1998.)...

Like the photosynthetic reaction center and bacteriorhodopsin, the bacterial ion channel also has tilted transmembrane helices, two in each of the subunits of the homotetrameric molecule that has fourfold symmetry. These transmembrane helices line the central and inner parts of the channel but do not contribute to the remarkable 10,000-fold selectivity for K+ ions over Na+ ions. This crucial property of the channel is achieved through the narrow selectivity filter that is formed by loop regions from thefour subunits and lined by main-chain carbonyl oxygen atoms, to which dehydrated K ions bind. 

In the polar pores, the diffusion coefficient of all ions is strongly reduced relative to the bulk values. No counterion dependence is observed for the SDC of CP. A more detailed analysis shows that the ion SDC depends on the ion s relative position in the pore [174]. In the case of the K ion, this dependence is particularly strong. K ions forming contact pairs with the surface charges are almost completely immobilized on the time scale of the simulations. The few remaining ions in the center of the pore are almost unaffected by the (screened) surface charges. The fact that most of the K ions form contact pairs substantially reduces the average value of the normalized K SDC to 0.2. The behavior of CP is similar to that of K. The SDC of sodium ions, which... 

Suppose that we arbitrarily set the partial molal entropy of the K+ ion equal to zero. This means that we assign to the Cl- ion the whole of the partial molal entropy of the ion pair (K+ + Cl-) that is to say, we assign to the Cl- ion, not only the unitary term for the Cl- ion, but also the cratic term for both ions, and also the unitary term for the potassium ion. 

The corresponding curve for the — T AS of ICCl, instead of lying below the curve for NaCl, as would be expected from simple electrostatic theory for an ion with a largor radius, rises considerably higher, as shown by the broken line at the top of Fig. 64. In Sec. 114 we suggested that this excess is due to the fact that, while the K+ ion produces order when dis-... 

Fig. 5. Tentative mixed potential model for the sodium-potassium pump in biological membranes the vertical lines symbolyze the surface of the ATP-ase and at the same time the ordinate of the virtual current-voltage curves on either side resulting in different Evans-diagrams. The scale of the absolute potential difference between the ATP-ase and the solution phase is indicated in the upper left comer of the figure. On each side of the enzyme a mixed potential (= circle) between Na+, K+ and also other ions (i.e. Ca2+ ) is established, resulting in a transmembrane potential of around — 60 mV. This number is not essential it is also possible that this value is established by a passive diffusion of mainly K+-ions out of the cell at a different location. This would mean that the electric field across the cell-membranes is not uniformly distributed.

Next, we find the molarity of K+ after the addition of K+ ions ... 

This half-reaction commonly occurs when the cation in solution is very difficult to reduce. For example, electrolysis of a solution containing K+ ions (E d = —2.936 V) or Na+ ions (E = —2.714 V) yields hydrogen gas at the cathode (Table 18.4). 

Explain in terms of nuclear charge why the K+ ion is smaller than the Cl- ion, though they are isoelectronic (they have the same number of electrons). 

Several facts become apparent. There are fewer Na+ ions than Cl- ions other positively charged ions—Mg+2, Ca+2, and K+—are also present. Sulfate ions, S04 2, and bromide ions, Br-, are other negatively charged ions present in the water. Thus, ocean water is more than a solution of sodium chloride. Another fact is that K+ ions are much less plentiful than Na+ ions (Na+/K+ is about 46) even though K+ ions are rather plentiful in the earth (Na+/K+ is about 2). 

The H,K-ATPase, expressed in the parietal cells of the stomach, transports H+ ion from cytoplasm to lumen in exchange for extracytoplasmic K+ ion in an electroneutral exchange using the energy of ATP hydrolysis. 

The catalytic cycle of the Na+/K+-ATPase can be described by juxtaposition of distinct reaction sequences that are associated with two different conformational states termed Ei and E2 [1]. In the first step, the Ei conformation is that the enzyme binds Na+ and ATP with very high affinity (KD values of 0.19-0.26 mM and 0.1-0.2 pM, respectively) (Fig. 1A, Step 1). After autophosphorylation by ATP at the aspartic acid within the sequence DKTGS/T the enzyme occludes the 3 Na+ ions (Ei-P(3Na+) Fig. la, Step 2) and releases them into the extracellular space after attaining the E2-P 3Na+ conformation characterized by low affinity for Na+ (Kq5 = 14 mM) (Fig. la, Step 3). The following E2-P conformation binds 2 K+ ions with high affinity (KD approx. 0.1 mM Fig. la, Step 4). The binding of K+ to the enzyme induces a spontaneous dephosphorylation of the E2-P conformation and leads to the occlusion of 2 K+ ions (E2(2K+) Fig. la, Step 5). Intracellular ATP increases the extent of the release of K+ from the E2(2K+) conformation (Fig. la, Step 6) and thereby also the return of the E2(2K+) conformation to the EiATPNa conformation. The affinity ofthe E2(2K+) conformation for ATP, with a K0.5 value of 0.45 mM, is very low. 

Potassium channels are a diverse and ubiquitous family of membrane proteins present in both excitable and nonexcitable cells that selectively conduct K+ ions across the cell membrane along its electrochemical gradient at a rate of 106-108 ions/s. 

About 78 human genes encoding a variety of K+ channels and auxiliary subunits have been identified (Fig. 1 Table 1). While the K+ channels are diverse, they share with a unique conducting pore highly selective for K+ ions. TheK+ channels ar e tetramers composed of four a subunits that form the conducting pore. On the basis of primary amino acid sequence of a subunit, K+ channels can be classified into three major families (Fig. 2). 

The inward rectifier K+ channels (Kir) represent this family of channels that conduct K+ ions preferentially in the inward direction than outward. The occlusion of internal vestibule oftheporeby Mg2+ and polyamines contribute to this inward rectification. These channels... 

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