Use the electronic configuration to explain the occurrence of period and groups to the periodic table.
1 answer:
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Answer:
27 min
Explanation:
The kinetics of an enzyme-catalyzed reaction can be determined by the equation of Michaelis-Menten:
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
Answer:
a) 2-bromopyrrole
Explanation:
Our options for this questions are:
a) 2-bromopyrrole
b) 2,3-dibromopyrrole
c) N-bromopyrrole
d) 3-bromopyrrole
To understand how the reaction works we have to start with the <u>resonance structures</u>. (Figure 1), on these structures, we will obtain a n<u>egative charge on carbon 2</u> in the pyrrole ring, therefore on this carbon we can generate an attack to an electrophile.
The second step is to check how the mechanism take place. An <u>electrophile is generated</u> by the and
. This electrophile can be <u>attacked</u> by the negative charge on carbon 2 producing the 2-bromopyrrole. (See figure 2).
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