Answer:
27 min
Explanation:
The kinetics of an enzyme-catalyzed reaction can be determined by the equation of Michaelis-Menten:
![v = \frac{vmax[S]}{Km + [S]}](https://tex.z-dn.net/?f=v%20%3D%20%5Cfrac%7Bvmax%5BS%5D%7D%7BKm%20%2B%20%5BS%5D%7D)
Where v is the velocity in the equilibrium, vmax is the maximum velocity of the reaction (which is directed proportionally of the amount of the enzyme), Km is the equilibrium constant and [S] is the concentration of the substrate.
So, initially, the velocity of the formation of the substrate is 12μmol/9min = 1.33 μmol/min
If Km is a thousand times smaller then [S], then
v = vmax[S]/[S]
v = vmax
vmax = 1.33 μmol/min
For the new experiment, with one-third of the enzyme, the maximum velocity must be one third too, so:
vmax = 1.33/3 = 0.443 μmol/min
Km will still be much smaller then [S], so
v = vmax
v = 0.443 μmol/min
For 12 μmol formed:
0.443 = 12/t
t = 12/0.443
t = 27 min
Two or more different elements
E and Dis determine the H
Answer:
Axial
Explanation:
In the most stable conformation of Cis-3-tert-Butylcyclohexanol, the tert-butyl group is at equatorial position and the alcohol group is in the axial position.
If the tert-butyl group is placed in equatorial position, repulsions are minimized. The bulkier the group, the greater the energy difference between the axial and equatorial conformers. Hence for a ring having a bulky substituent, such bulky substituent is better placed in the equatorial position.
The energy difference between the conformers of Cis-3-tert-Butylcyclohexanol is so high that the compound is almost "frozen" in a conformation where the tert-butyl groups are equatorial and the -OH groups are axial. This conformer is more stable by 24 KJ/mol.