Answer:
It's spontaneous in the reverse direction
Explanation:
A negative voltage indicate s that the reverse reaction is spontaneous (i.e. oxidation at the cathode, and reduction at the anode; by convention you would need to swap the labels on the electrodes)
Aluminum or glass I think
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
Sodium Sulfate
= Na2(SO4) meaning there are two ions of Na+ in one mole of Sodium Sulfate the M
stands for Molarity, defined as Molarity = (moles of solute)/(Liters of
solution), So if the Na2SO4 solution is 3.65M that means one Liter of has 3.65
moles of Na2SO4, the stoichiometry of Na2SO4 shows that there would be two Na+
ions in solution for every one Na2SO4.
Therefore if
3.65 moles of Na2SO4 was to dissolve, it would produce 7.3 moles of Na+, and
since this is still a theoretical solution, we can assume 1 L of solution.
Finally we find
[Na+] = 2*3.65 = 7.3M
Use the same
logic for parts b and c
