Using the Michaelis-Menten equation competitive inhibition, the Inhibition constant, Ki of the inhibitor is 53.4 μM.
<h3>What is the Ki for the inhibitor?</h3>
The Ki of an inhibitor is known as the inhibition constant.
The inhibition is a competitive inhibition as the Vmax is unchanged but Km changes.
Using the Michaelis-Menten equation for inhibition:
Making Ki subject of the formula:
where:
- Kma is the apparent Km due to inhibitor
- Km is the Km of the enzyme-catalyzed reaction
- [I] is the concentration of the inhibitor
Solving for Ki:
where
[I] = 26.7 μM
Km = 1.0
Kma = (150% × 1 ) + 1 = 2.5
Ki = 26.7 μM/{(2.5/1) - 1)
Ki = 53.4 μM
Therefore, the Inhibition constant, Ki of the inhibitor is 53.4 μM.
Learn more about enzyme inhibition at: brainly.com/question/13618533
The type of reaction that occurs without the addition of heat is called spontaneous reaction. That is option D.
<h3>What is spontaneous reaction?</h3>
Spontaneous reaction is defined as the reaction where by new substances are formed naturally without the addition of extra energy in the form of heat.
Therefore, the type of reaction that occurs without the addition of heat is called spontaneous reaction
Learn more about heat here:
brainly.com/question/13439286
#SPJ1
the balanced equation for the formation of ammonia is
N₂ + 3H₂ ---> 2NH₃
molar ratio of N₂ to NH₃ is 1:2
mass of N₂ reacted is 8.0 g
therefore number of N₂ moles reacted is - 8.0 g / 28 g/mol = 0.286 mol
according to the molar ratio,
1 mol of N₂ will react to give 2 mol of NH₃, assuming nitrogen is the limiting reactant
therefore 0.286 mol of N₂ should give - 2 x 0.286 mol = 0.572 mol of NH₃
therefore mass of NH₃ formed is - 0.572 mol x 17 g/mol = 9.72 g
a mass of 9.72 mol of NH₃ is formed
