Answer:
A
Explanation:
10,000g
just multiply the amount of hectograms by 100 to get grams
When we balance the given equation
SF₆(g) + SO₃(g) → SO₂F₂(g)
We will get
SF₆(g) + 2SO₃(g) → 3SO₂F₂(g)
Solution:
Balancing the given equaation
SF₆(g) + SO₃(g) → SO₂F₂(g)
We have to balance the given number of O
SF₆(g) + 2SO₃(g) → 3SO₂F₂(g)
We get balanced equation
SF₆(g) + 2SO₃(g) → 3SO₂F₂(g)
The reaction quotient will be
Qc = [product] / [reactant]
Qc = [SO₂F₂(g)] / [SF₆(g) + SO₃(g)]
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Answer:
From least polar covalent to most polar covalent;
S-I< Br-Cl < N-H< Te-O
From most ionic to least ionic
Cs-F> Sr-Cl> Li- N> Al-O
Explanation:
Electro negativity refers to the ability of an atom in a bond to attract the shared electrons of the bond towards itself.
Electro negativity difference between two atoms is a key player in the nature of bond that exists between any two atoms. A large difference in electron negativity leads to an ionic bond while an intermediate difference in electro negativity leads to a polar covalent bond.
Based on electro negativity differences, the bonds in the answer have been arranged in order of increasing polar covalent nature or decreasing ionic nature.
Answer:
1.56 mol H₂
Explanation:
Mg₃(Si₂O₅)₂(OH)₂
<em>There are 4 Si moles per Mg₃(Si₂O₅)₂(OH)₂ mol</em>. With that in mind we can <u>calculate how many Mg₃(Si₂O₅)₂(OH)₂ moles are there in the sample</u>, using the <em>given number of silicon moles</em>:
- 3.120 mol Si *
= 0.78 mol Mg₃(Si₂O₅)₂(OH)₂
Then we can <u>convert Mg₃(Si₂O₅)₂(OH)₂ moles into hydrogen moles</u>, keeping in mind that <em>there are 2 hydrogen moles per Mg₃(Si₂O₅)₂(OH)₂ mol</em>:
- 0.78 mol Mg₃(Si₂O₅)₂(OH)₂ * 2 = 1.56 mol H₂
Answer:
Michaelis constant is known as km which is the substrate concentration that encourages the compound to work at half maximum velocity represented by Vmax/2. Michaelis constant is inversely related to the substrate and the affinity of the enzyme.
Induced fit model: The premise of the purported induced fit hypothesis, which expresses that the attachment or association of a substrate or some other atom to an enzyme causes an adjustment to the enzyme in order to fit or restrain its activity.
In substrate, analog Km or Michaelis constant will be high as the substrate will stay because of analogs inhibit activity.
In the transitional state, analog Km will be in the middle of the substrate and product analogs. Progress state analogs are synthetic mixes with a structure catalyzed reaction that looks like the progressing condition of a substrate atom in a compound enzyme.
In item simple thus Km is the least.
0.0013 M = product ananlog,
0.025 M=Transition state, and
0.0045 M = Substrate analog
