Answer:
c. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron.
e. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ( Fe ) (Fe) atom.
f. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. The heme prosthetic group is entirely buried within myoglobin.
Explanation:
The differences between hemoglobin and myoglobin are most important at the level of quaternary structure. Hemoglobin is a tetramer composed of two each of two types of closely related subunits, alpha and beta. Myoglobin is a monomer (so it doesn't have a quaternary structure at all). Myoglobin binds oxygen more tightly than does hemoglobin. This difference in binding energy reflects the movement of oxygen from the bloodstream to the cells, from hemoglobin to myoglobin.
Myoglobin binds oxygen
The binding of O 2 to myoglobin is a simple equilibrium reaction:
An ionic bond is composed of a cation and anion, which are charged ions. You cannot have atoms with ionic bonds, because there is no opposite attraction between charges due to atoms having a net nuclear charge of zero. Therefore, a cation and anion would most likely be joined by an ionic bond.
Answer:
Your answer should be 15.68 grams.
Explanation:
Seeing as 1 mole has a mass of 56 g, 56*0.28 would get you 15.68 g.
Octet means presence of a total of 8 electrons in its valence shell while in case of duplet only 2 electrons are present in valence shell.
<u>Answer:</u> The molality of the solution is 0.1 m.
<u>Explanation:</u>
To calculate the molality of solution, we use the equation:
Where,
= Given mass of solute = 27.1 g
= Molar mass of solute = 27.1 g/mol
= Mass of solvent = 100 g
Putting values in above equation, we get:
Hence, the molality of the solution is 0.1 m.
