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Release steps

The specific effect of actin on myosin ATPase becomes apparent if the product release steps of the reaction are carefully compared. In the absence of actin, the addition of ATP to myosin produces a rapid release of H, one of the products of the ATPase reaction ... [Pg.552]

The crossbridge cycle in muscle. Myosin crossbridges interact cyclically with binding sites on actin filaments. Note that the energy release step—when ATP is broken down to ADP—recocks the crossbridge head. [Pg.174]

The theoretical approach involved the derivation of a kinetic model based upon the chiral reaction mechanism proposed by Halpem (3), Brown (4) and Landis (3, 5). Major and minor manifolds were included in this reaction model. The minor manifold produces the desired enantiomer while the major manifold produces the undesired enantiomer. Since the EP in our synthesis was over 99%, the major manifold was neglected to reduce the complexity of the kinetic model. In addition, we made three modifications to the original Halpem-Brown-Landis mechanism. First, precatalyst is used instead of active catalyst in om synthesis. The conversion of precatalyst to the active catalyst is assumed to be irreversible, and a complete conversion of precatalyst to active catalyst is assumed in the kinetic model. Second, the coordination step is considered to be irreversible because the ratio of the forward to the reverse reaction rate constant is high (3). Third, the product release step is assumed to be significantly faster than the solvent insertion step hence, the product release step is not considered in our model. With these modifications the product formation rate was predicted by using the Bodenstein approximation. Three possible cases for reaction rate control were derived and experimental data were used for verification of the model. [Pg.28]

The product elimination step at extremely low temperatures (< -40°C) was reported as the rate-controlling step (3). However, when the reaction is run at room temperature, this step is assumed to be much faster than the solvent insertion step (k4 ks). Hence this product release step can be neglected. This simplification has been applied for asymmetric hydrogenation and published in the literature (10). [Pg.29]

Step I Template release Step 2 T emplate rebinding ... [Pg.189]

This methodology clearly enriches the tool box of the synthetic organic chemist. Other spin-offs from the studies described above, such as the incorporation of dioxygen as an oxidant and the use of alkyl carbon-het-eroatom coupling as a product release step for other metal-mediated organic transformations, may also emerge over the next several years. [Pg.313]

The rate constants from this study are given in Table V. The kinetic data show that intercalation steps (steps 1 and 2) are responsible for the observed catalyzed hydrolysis. The much slower product release step (.step 3), occuring over hours and not associated with the observed relaxations, is the rate limiting step. [Pg.250]

In this mechanism, the protomer addition and release steps are exclusively taking place at opposite ends of the tubule. [Pg.201]

An enzyme-catalyzed reaction scheme in which the two substrates (A and B) can bind in any order, resulting in the formation of a single product of the enzyme-catalyzed reaction (hence, this reaction is the reverse of the random Uni Bi mechanism). Usually the mechanism is distinguished as to being rapid equilibrium (/.c., the ratedetermining step is the central complex interconversion, EAB EP) or steady-state (in which the substrate addition and/or product release steps are rate-contributing). See Multisubstrate Mechanisms... [Pg.602]

Habib (4) has emphasized the importance of the sulfur-release step in the mechanism for SOx reduction. If a catalyst captures SOx but cannot release it, it soon becomes saturated and ineffective. For example, if CaO captured SOx until it was transformed to CaSO, it would capture 57% sulfur, based on the weight of the CaO. For the FCCU under consideration, 50 tons of CaO added to the 500-ton unit (10% additive) would capture 28.6 tons of sulfur. At a sulfur capture rate of 10 tons a day, the CaO would be effective for only 2.9 days. Since the average catalyst residence time in the unit is 100 days, use of such a material would not be practical. [Pg.150]

The latter number incorporates just the chemical step(s) of formation of triazole within cucurbituril. Since the product release step apparently is at least 100-fold slower than the actual cycloaddition, the net catalytic acceleration should be adjusted downward by that amount. An instructive alternative estimation of kinetic enhancement is to compare the extrapolated limiting rate for cycloaddition within the complex (i.e. cucurbituril saturated with both reactants, k — 1.9xl0 s ) with the uncatalyzed unimolecular transformation of an appropriate bifunctional reference substrate as in Eq. (3) (k, = 2.0x 10 s ). Such a comparison of first-order rate constants shows that the latter reaction is approximately a thousandfold slower than the cucurbituril-engendered transformation. This is attributable to necessity for freezing of internal rotational degrees of freedom that exist in the model system, which are taken care of when cucurbituril aligns the reactants, and concomitantly to an additional consideration which follows. [Pg.19]

After the U1 snRNP binds to the pre-mRNA (step a, Fig. 28-22)614 the U2 snRNP binds to another almost invariant sequence CURACU found 20 to 55 nucleotides upstream of the 3 junction.608,615-617 The A in this sequence becomes a branch point. It is brought close to the 5 splice site with the aid of a preassembled complex of snRNPs U4, U6, and U5. In this complex U4 and U6 are tightly paired, additional proteins are also present,618 21 and enhancers may be located in adjacent exons.617 Upon binding of U6 to the 5 splice site, the U1 and U4 snRNPs are released (step b, Fig. 28-22) and the 2 -OH of the branch point adenosine attacks the backbone phosphorus atom (step c) at the 5 splice junction forming a lariat intermediate. The 3 end created at the 5 junction must now be held and brought close to the 3 splice junction, which is located with the aid of U5 snRNP.622 The 3 splice junction, utilized in the second splicing step (step d, Fig. 28-22) has the consensus sequence (T/C)N(C/T)AG G. [Pg.1647]

Michaelis-Menten approach (Michaelis and Menten, 1913) It is assumed that the product-releasing step, Eq. (2.6), is much slower than the reversible reaction, Eq. (2.5), and the slow step determines the rate, while the other is at equilibrium. This is an assumption which is often employed in heterogeneous catalytic reactions in chemical kinetics.3 Even though the enzyme is... [Pg.13]

The Michaelis-Menten approach assumes that the product releasing step is much slower than the first complex forming step of the simple enzyme-reaction mechanism ... [Pg.42]

Derive a rate equation for the case in which the enzyme-substrate formation step is much slower than the product releasing step, that is, Jq k3, k2 k3. State your assumptions. [Pg.42]

Bagshaw, C. R., and Trentham, D. R. (1974). The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction. Biochem.J. 141, 331-349. [Pg.189]

White, H. D., Belknap, B., and Webb, M. R. (1997). Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate. Biochemistry 36, 11828-11836. [Pg.194]

In various cases, the release step is accompanied by a cyclization leading to heterocycles. It should be noted that under these conditions parts of the linker can become part of the product which is released into solution. [Pg.269]

Generally there is one reaction in the complex scheme one writes for combustion gases that is the main energy releasing step. This reaction then becomes the reaction of concern in the Bray approach. [Pg.137]

Amplification of the captured sequence can be performed directly on cationic hydrophilic particles without a release step, since they are compatible with the amplification medium, such as PCR (Polymerase Chain Reaction), or after a desorption step and the removal of colloidal particles. [Pg.190]

FIGURE 3.5 One of the postulated pathways for the 02 release step of the WOC. The naturally occurring WOC of photosystem II is able to efficiently photooxidize water in a sustainable manner using visible light according to the reaction 2 HzO —> 02 + 4 H+ + 4 e. SOURCE Presented by Charles Dismukes. [Pg.33]

In all these experimental models, the MTX effect could be divided in three phases (1) a rapidly developing Ca conductance through NSCC (2) uptake of vital dyes (ethidium, YO-PRO and POPO-3) and Fura-2 loss via a cytolitic-oncotic pore (COP) and (3) a secondaiy phase of vital dye uptake and Fura loss in which membrane permeability to larger molecules like LDH enzyme occurs. Fig. 4.4 shows permeability changes in a population study of bovine aortic endothehal cells (BAECs) treated with 0.3 nM MTX. Two phases of ethidium bromide uptake may be observed (steps 2 and 3 of the death process), the second phase correlating in time with LDH release (step 3 of death process). [Pg.66]

For the network taken at face value, eqn 8.81 with appropriately changed indices, irreversible diol release steps, and X2 and X4 as lacs (so that 6 = Dm + Dn and = >33) gives... [Pg.241]


See other pages where Release steps is mentioned: [Pg.227]    [Pg.11]    [Pg.577]    [Pg.121]    [Pg.307]    [Pg.59]    [Pg.217]    [Pg.199]    [Pg.59]    [Pg.1005]    [Pg.67]    [Pg.180]    [Pg.751]    [Pg.39]    [Pg.14]    [Pg.282]    [Pg.261]    [Pg.187]    [Pg.124]    [Pg.217]    [Pg.69]    [Pg.221]    [Pg.61]    [Pg.58]    [Pg.116]    [Pg.7]    [Pg.121]    [Pg.139]   
See also in sourсe #XX -- [ Pg.478 ]




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