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Stells [14]
3 years ago
11

When a 3.25 g sample of solid sodium hydroxide was dissolved in a calorimeter in 100.0 g of water, the temperature rose from 23.

9 °C to 32.0 °C. Calculate ∆H (in kJ/mol) for the solution process: NaOH (s) → Na+ (aq) + OH- (aq)
Use a calorimeter heat capacity of Ccal = 15.8 J/°C
Chemistry
1 answer:
sertanlavr [38]3 years ago
4 0

Answer : The enthalpy change for the solution is 42.8 kJ/mol

Explanation :

Heat released by the reaction = Heat absorbed by the calorimeter + Heat absorbed by the water

q=[q_1+q_2]

q=[c_1\times \Delta T+m\times c_2\times \Delta T]

where,

q = heat released by the reaction

q_1 = heat absorbed by the calorimeter

q_2 = heat absorbed by the water

c_1 = specific heat of calorimeter = 15.8J/^oC

c_2 = specific heat of water = 4.18J/g^oC

m = mass of water = 100.0 g

\Delta T = change in temperature = T_2-T_1=(32.0-23.9)=8.1^oC

Now put all the given values in the above formula, we get:

q=[(15.8J/^oC\times 8.1^oC)+(100.0g\times 4.18J/g^oC\times 8.1^oC)]

q=3513.8J=3.5138kJ        (1 kJ = 1000 J)

Now we have to calculate the enthalpy change for the solution.

\Delta H=\frac{q}{n}

where,

\Delta H = enthalpy change = ?

q = heat released = 3.5138 kJ

m = mass of NaOH = 3.25 g

Molar mass of NaOH = 40 g/mole

\text{Moles of }NaOH=\frac{\text{Mass of }NaOH}{\text{Molar mass of }NaOH}=\frac{3.25g}{40g/mole}=0.0812mole

Now,

\Delta H=\frac{3.5138kJ}{0.0821mole}=42.8kJ/mol

Therefore, the enthalpy change for the solution is 42.8 kJ/mol

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Complete Question

The complete question is shown on the first uploaded image

Answer:

[S]<<KM             |   [S]=KM                  |  [S]>>KM                     | Not true

____________  |   Half of the active  | Reaction rate is         | Increasing

[E_{free}] is about   |    sites are filled of  |    independent of      |  [E_{Total}] will                                            

 equal to [E_{total}]. |                                 |   [S]                             | lower KM

_____________________________________________|____________

[ES] is much       |                                 | Almost all active

 lower than         |                                 | sites are filled

[E_{free}]                  |                                 |

Explanation:

Generally the combined enzyme[ES] is mathematically represented as

                   [ES] = \frac{[E_{total}][S]}{K_M + [S]}----(1)

for Michaelis-Menten equation

Where [S] is the substrate concentration and K_M is the Michaelis constant

Considering the statement [S] < < K_M

  Looking at the equation [S] is denominator so it can be ignored(it is far too small compared to K_M)  hence the above equation becomes

               [ES] = \frac{[E_{total}][S]}{K_M}

Since [S] is less than K_M it means that \frac{[S]}{K_M}  < < 1

so it means that [ES] < < [E_{total}]

  What this means is that the  number of combined enzymes[ES] i.e the number of occupied site is very small compared to the the total sites [E_{total}]  i.e the total enzymes concentration which means that the free sites [E_{free}]  i.e the concentration of free enzymes is almost equal to [E_{total}]

Considering the second statement

      [S] = K_M

So  this means that equation one would now become

           [ES] = \frac{[E_{total}][S]}{2[S]} = \frac{[E_{total}]}{2}

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Considering the Third Statement

      [S] >>K_M

In this case the K_M in the denominator of equation 1 would be neglected and the equation becomes

       [ES] = \frac{[E_{total}] [S]}{[S]} = [E_{total}]

This means that almost all the sites are occupied with substrate

 The rate of this reaction is mathematically defined as

             v =\frac{V_{max}[S]}{K_M [S]}

Where v is the rate of the reaction(also know as the velocity of the reaction at a given time t) and V_{max}  is he maximum velocity of the reaction

In this case also the K_M at the denominator would be neglected as a result of the statement hence the equation becomes

                v = \frac{V_{max}[S]}{[S]} = V_{max}

So it means that the reaction does not depend on the concentration of substrate [S]

For the final statement(Not True ) it would match with condition that states that increasing [E_{total}] will lower K_M

This is because K_M does not depend on enzyme concentration it is a property of a enzyme

             

       

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