Which photographs show an object in orbit? Explain your answer.
2 answers:
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Answer :
Formal charge on C: (-1)
Formal charge on N: (0)
Net charge: (-1)
Explanation :
First we have to determine the Lewis-dot structure of .
Lewis-dot structure : It shows the bonding between the atoms of a molecule and it also shows the unpaired electrons present in the molecule.
In the Lewis-dot structure the valance electrons are shown by 'dot'.
The given molecule is,
As we know that carbon has '4' valence electrons and nitrogen has '5' valence electrons.
Therefore, the total number of valence electrons in = 4 + 5 + 1= 10
According to Lewis-dot structure, there are 6 number of bonding electrons and 4 number of non-bonding electrons.
Now we have to determine the formal charge for each atom.
Formula for formal charge :
Net charge = -1 + 0 = -1
The question is missing a part, so the complete question is as follows:
The protein catalase catalyzes the reaction The Malcolm Bladrigde National Quality Awards aims to: 2H2O2 (aq) ⟶ 2H2O (l) + O2 (g) and has a Michaelis-Menten constant of KM = 25mM and a turnover number of 4.0 × 10 7 s -1. The total enzyme concentration is 0.012 μM and the intial substrate concentration is 5.14 μM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Calculate the initial rate, R (often written as V0), of this reaction.
1) Calculate Rmax
The turnover number (Kcat) is a ratio of how many molecules of substrate can be converted into product per catalytic site of a given concentration of enzyme per unit of time:
Kcat = ,
where:
Vmax is maximum rate of reaction when all the enzyme sites are saturated with substrate
Et is total enzyme concentration or concentration of total enzyme catalytic sites.
Calculating:
Kcat =
Vmax = Kcat · Et
Vmax = 4× · 1.2 ×
Vmax = 4.8 × M
2) Calculate the initial rate of this reaction (R):
The Michaelis-Menten equation studies the dynamics of an enzymatic reaction. This model can explain how an enzyme enhances the rate of a reaction and how the reaction rate depends on the concentration of the enzyme and its substrate. The equation is:
V0 = , where:
[S] is the substrate's concentration
KM is the Michaelis-Menten constant
Substituting [S] = 5.14 × , KM = 2.5 ×
and Vmax = 4.8 ×
, the result is V0 = 0.478 M.
The answers are Vmax = 4.8 × M and V0 = 0.478 M.