Answer: 7s
Explanation:
The order of the reaction is 2.
Integrated rate law for second order kinetic is determined using the formula
1/[At]=1/[Ao] +kt
But, [Ao] is the initial concentration = 1.50 mol/L
And [At] is the final concentration = 1/3 of initial concentration =1/3×1.5 = 0.5 mol/L
Rate constant, k = 0.2 L/mol*s
Using the formula
1/0.5=1/1.5+0.2t
Collecting like terms
1/0.5-1/1.5=0.2t
LCM = 1.5
3-1/1.5=0.2t
2/1.5=0.2t
Multiply both sides by 1/0.2
2/1.5×0.2=t
2/0.3=t
t=6.66s
t=7s
Answer: The value of the equilibrium constant Kc for this reaction is 3.72
Explanation:
Equilibrium concentration of 
= 
Equilibrium concentration of 
= 
Equilibrium concentration of 
= 
Equilibrium concentration of 
= 
Equilibrium constant is defined as the ratio of concentration of products to the concentration of reactants each raised to the power their stoichiometric ratios. It is expressed as 
For the given chemical reaction:
The expression for is written as:
![K_c=\frac{[NO_2]^3\times [H_2O]^1}{[HNO_3]^2\times [NO]^1}](https://tex.z-dn.net/?f=K_c%3D%5Cfrac%7B%5BNO_2%5D%5E3%5Ctimes%20%5BH_2O%5D%5E1%7D%7B%5BHNO_3%5D%5E2%5Ctimes%20%5BNO%5D%5E1%7D)
Thus the value of the equilibrium constant Kc for this reaction is 3.72
<h3>
Answer:</h3>
1. Irreversible Inhibition-Inhibitor may permanently modify an enzyme
2. Irreversible inhibition- Tamiflu, a transition state analog, reversibly binds to neuraminindase
3. Competitive Inhibition-Inhibitor binds reversibly to an enzyme's active
4.Irreversible inhibition-Inhibitor binds to an enzyme at a site other than active site
5. Mixed inhibition-The Al3+ ion binds to acetylcholinesterase or to the acetylcholinesterase- substrate complex
6. Irreversible inhibition-DIPF permanently modifies the hydroxyl group of a Serine residue at the active site
<h3>
Explanation:</h3>
- An enzyme is a biological catalyst that catalysis chemical reactions.
- Enzyme activity is influenced by several factors which include enzyme inhibitors, temperature, and pH among others.
- Enzyme inhibitors are molecules that bind to the enzyme thus interfering with enzyme activity and preventing the binding of substrate to the enzyme.
- Inhibitors may either irreversibly or reversibly bind the enzymes.
- Competitive inhibitors compete with substrates for the active sites while non-competitive inhibitors bind irreversibly to other sites on the enzyme other than the active site.
- Tamiflu is an example of a competitive inhibitor.
- DIPF is an example of a non-competitive inhibitor as it binds the enzyme permanently.
