Resting states

Figure C3.6.7(a) shows tire u= 0 and i )= 0 nullclines of tliis system along witli trajectories corresponding to sub-and super-tlireshold excitations. The trajectory arising from tire sub-tlireshold perturbation quickly relaxes back to tire stable fixed point. Three stages can be identified in tire trajectory resulting from tire super-tlireshold perturbation an excited stage where tire phase point quickly evolves far from tire fixed point, a refractory stage where tire system relaxes back to tire stable state and is not susceptible to additional perturbation and tire resting state where tire system again resides at tire stable fixed point.

Fibroelastic Fibrous material possessing elastic properties. In the airway, fi-broelastic tissue throughout the lung contributes to its overall elasticity, generating a positive recoil force at the functional residual capacity, or resting state of the lungs. 

The P450 reaction cycle (Scheme 10.4) starts with four stable intermediates that have been characterized by spectroscopic methods. The resting state of the enzyme is a six-coordinate, low-spin ferric state (complex I) with water (or hydroxide) coordinated trans to the cysteinate ligand. The spin state of the iron changes to high-spin upon substrate binding and results in a five-coordinate ferric ion (com-... 

Like other voltage-gated cation channels, Ca2+ channels exist in at least three states A resting state stabilized at negative potentials (such as the resting potentials of most electrically excitable cells) that is a closed state from which the channel can open. The open state is induced by depolarization. Channels do not stay open indefinitely because they are turned off during prolonged depolarization by transition into an inactivated state. Inactivation is driven both by depolarization... 

Kv-channels are closed in the resting state. Upon depolarization of the cellular membrane potential, closed Kv-channels undergo a series of voltage-dependent activating steps until they reach an activated state from which they can open and close in a voltage-independent manner. 

It is usually presumed that smooth muscle cells have only one kind of activity, contraction, and that the only alternative to contractile activity is a kind of estivating resting state (Figure 11). The actual situation is of course more complicated. For example, smooth muscles synthesize extracellular filament protein. They also proliferate, particularly in the cardiovascular system. Both of these processes require a considerable amount of control of the cellular economy. 

The rate of respiration of mitochondria can be controlled by the availability of ADP. This is because oxidation and phosphorylation are tightly coupled ie, oxidation cannot proceed via the respiratory chain without concomitant phosphorylation of ADP. Table 12-1 shows the five conditions controlling the rate of respiration in mitochondria. Most cells in the resting state are in state 4, and respiration is controlled by the availability of ADP. When work is performed, ATP is converted to ADP, allowing more respiration to occur, which in turn replenishes the store of ATP. Under certain conditions, the concentration of inorganic phosphate can also affect the rate of functioning of the respiratory chain. As respiration increases (as in exercise). 

In the sarcoplasm of resting muscle, the concentration of Ca + is 10 to 10 mol/L. The resting state is achieved because Ca + is pumped into the sarcoplasmic reticulum through the action of an active transport system, called the Ca + ATPase (Figure 49-8), initiating relaxation. The sarcoplasmic reticulum is a network of fine membranous sacs. Inside the sarcoplasmic reticulum, Ca + is bound to a specific Ca -binding protein designated calsequestrin. The sarcomere is surrounded by an excitable membrane (the T tubule system) composed of transverse (T) channels closely associated with the sarcoplasmic reticulum. 

Activation is slower in less depolarized membranes and inactivation drains the open (and resting) state more effectively. In fact, real Na" " channels gate by more complex pathways, including several closed states intermediate between R and O, as well as multiple inactivated states. Inactivation from these intermediate states is probably faster than from / , and the entire activation process, in its fully branched entirety, is rich with kinetic possibilities. However, the effects of toxins may be understood in general by the simpler scheme presented in Figure 2. 

Equally to ferrate 38 ferrates 39 and 40 also catalyze Alder-ene cycloisomeriza-tions [17]. Compared to 38, they require somewhat longer reaction times, possibly due to the chelating cod-hgand, which is more difficult to substitute by the en)me. The presence of cod in the reaction turns out to be of advantage with more demanding substrates like acyclic enynes with a terminal aUcene moiety where ferrate 38 is not reactive. Cod is assumed to stabilize the catalyst in its resting state as ancillary hgand. 

Duba AG, K Jackson, MC Jovanovich, RB Knapp, RT Taylor (1996) TCE remediation using in situ resting-state bioaugmentation. Environ Sci Technol 30 1982-1989. 

In most cases, the dppe complex decomposed rapidly, but the more robust dcpe derivative was observed to be the catalyst resting state by NMR. Smaller phosphines reacted more quickly but less selectively in these systems, and selectivity for the hydrophosphination products ranged from 29 to >95%. It is likely that the phosphine byproducts included telomers such as 1 (Scheme 54), but they were not characterized. [9]... 

In the thermodynamically redox-stable resting state, CcOs all Cu ions are in the Cu state and all hemes are Fe . From this state, CcOs can be reduced by one to four electrons. One-electron reduced CcOs are aerobically stable with the electron delocalized over the Cua and heme a sites. The more reduced forms—mixed-valence (two-electron reduced), three-electron reduced, and fully (four-electron) reduced—bind O2 rapidly and reduce it to the redox level of oxide (—2 oxidation state) within <200 p-s [Wikstrom, 2004 Michel, 1999]. This rate is up to 100 times faster than the average rate of electron transfer through the mammalian respiratory chain under normal... 

Figure 18.11 Plausible catalytic cycle for the ORR by simple Fe porphyrins adsorbed on the electrode surface and side Reactions (18.15)-(18.18). At pH < 3, the resting state of the catalyst is assumed to be ferric-aqua.

Only three steps of the proposed mechanism (Fig. 18.20) could not be carried out individually under stoichiometric conditions. At pH 7 and the potential-dependent part of the catalytic wave (>150 mV vs. NHE), the —30 mV/pH dependence of the turnover frequency was observed for both Ee/Cu and Cu-free (Fe-only) forms of catalysts 2, and therefore it requires two reversible electron transfer steps prior to the turnover-determining step (TDS) and one proton transfer step either prior to the TDS or as the TDS. Under these conditions, the resting state of the catalyst was determined to be ferric-aqua/Cu which was in a rapid equilibrium with the fully reduced ferrous-aqua/Cu form (the Fe - and potentials were measured to be within < 20 mV of each other, as they are in cytochrome c oxidase, resulting in a two-electron redox equilibrium). This first redox equilibrium is biased toward the catalytically inactive fully oxidized state at potentials >0.1 V, and therefore it controls the molar fraction of the catalytically active metalloporphyrin. The fully reduced ferrous-aqua/Cu form is also in a rapid equilibrium with the catalytically active 5-coordinate ferrous porphyrin. As a result of these two equilibria, at 150 mV (vs. NHE), only <0.1%... 

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