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:
Explanation:
mass H2O2 = 55 mL(1.407 g/mL) = 80.85 g
molar mass H2O2 = 2(1.01 g/mol) + 2(16.00 g/mol) = 34.02 g/mol
moles H2O2 = 80.85 g/34.02 g/mol = 2.377 moles H2O2
For each mole of H2O2 you obtain 0.5 mole of O2 (see the equation).
moles O2 = 2.377 moles H2O2 (1 mole O2)/(2 moles H2O2) = 1.188 moles O2
Now, you need the temperature. If you are at STP (273 K, and 1.00 atm) then 1 mole of an ideal gas at STP has a volume of 22.4 L. Without temperature you are not really able to continue. I will assume you are at STP.
Volume O2 = 1.188 moles O2(22.4 L/mole) = 0.0530 L of O2.
which is 53 mL.
Answer:
thé answer is b ) electronegativity
