The proton transfer reaction between Cyanide and water can be written as; X^- + H2O -----> HX + OH^-
<h3>What is a proton transfer reaction?</h3>
A proton transfer reaction is one in which a proton is moved from one chemical specie to another.It is in fact and acid - base reaction in the Brownstead - Lowry sense.
The proton transfer reaction between Cyanide and water can be written as(Let the cyanide ion be shown as X);
X^- + H2O -----> HX + OH^-
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group 1 elements are metals with<u> low</u> density
The rate constant of first order reaction at 32. 3 °C is 0.343 /s must be less the 0. 543 at 25°C.
First-order reactions are very commonplace. we have already encountered examples of first-order reactions: the hydrolysis of aspirin and the reaction of t-butyl bromide with water to present t-butanol. every other reaction that famous obvious first-order kinetics is the hydrolysis of the anticancer drug cisplatin.
The value of ok suggests the equilibrium ratio of products to reactants. In an equilibrium combination both reactants and merchandise co-exist. big ok > 1 merchandise are k = 1 neither reactants nor products are desired.
Rate constant K₁ = 0. 543 /s
T₁ = 25°C
Activation energy Eₐ = 75. 9 k j/mol.
T₂ = 32. 3 °C.
K₂ =?
formula;
log K₂/K₁= Eₐ /2.303 R [1/T₁ - 1/T₂]
putting the value in the equation
K₂ = 0.343 /s
Hence, The rate constant of first order reaction at 32. 3 °C is 0.343 /s
The specific rate steady is the proportionality consistent touching on the fee of the reaction to the concentrations of reactants. The fee law and the specific charge consistent for any chemical reaction should be determined experimentally. The cost of the charge steady is temperature established.
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Answer:
A noncompetitive inhibitor can only bind to an enzyme with or without a substrate at several places at a particular point in time
Explanation:
this is because It changes the conformation of an enzyme as well as its active site, which makes the substrate unable to bind to the enzyme effectively so that the efficiency of the enzyme decreases. A noncompetitive inhibitor binds to the enzyme away from the active site, altering/distorting the shape of the enzyme so that even if the substrate can bind, the active site functions less effectively and most of the time also the inhibitor is reversible
