0.114 mol/l
The equilibrium equation will be:
Kc = ([Br2][Cl2])/[BrCl]^2
The square factor for BrCl is due to the 2 coefficient on that side of the equation.
Now solve for BrCl, substitute the known values and calculate.
Kc = ([Br2][Cl2])/[BrCl]^2
[BrCl]^2 * Kc = ([Br2][Cl2])
[BrCl]^2 = ([Br2][Cl2])/Kc
[BrCl] = sqrt(([Br2][Cl2])/Kc)
[BrCl] = sqrt(0.043 mol/l * 0.043 mol/l / 0.142)
[BrCl] = sqrt(0.001849 mol^2/l^2 / 0.142)
[BrCl] = sqrt(0.013021127 mol^2/l^2)
[BrCl] = 0.114110152 mol/l
Rounding to 3 significant figures gives 0.114 mol/l
Answer:
Because it only needs one more electron to get to a full valence shell (8), so it really wants it and is pulling other electrons in. It also has to do with needing one more electron to fill the 2p shell. It is a small element which means its electrons are pulled tightly to the nucleus.
Hope this helps!
Explanation:
D. a compound can only be separated into its components by chemical means
Answer:
The correct answer is: Serine, Histidine, Aspartate
Explanation:
The catalytic triad of an enzyme is composed of three aminoacid residues which are the most important for its catalytic activity. They are located in the catalytic site of the enzyme. In the case of chymotrypsin- a serine protease, the catalytic triad is composed by serine, histidine and aspartate (Ser-His-Asp). Serine proteases hydrolyse peptidic bonds in proteins and peptides. To do that, the histidine-which interacts with the aspartate by a hydrogen bond so its pKa increases- take a proton from the serine. Thus, deprotonated serine is able to attack the peptide bond and to perform hydrolysis.
