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:
Answer:
0.0845 M
Explanation:
First we <u>convert 4.27 grams of potassium iodide into moles</u>, using its <em>molar mass</em>:
- Molar Mass of KI = 166 g/mol
- 4.27 g ÷ 166 g/mol = 0.0257 mol
Now we <u>calculate the molarity of the solution</u>, using <em>the number of moles and the given volume</em>:
- Molarity = moles / liters
- Molarity = 0.0257 mol / 0.304 L = 0.0845 M
Answer:
T = 9.875K
Explanation:
The ideal gas Law is PV = nRT.
P = Pressure
V = Volume
n = amount of substance
R = 8.314 J/(K. mol)
T = Temperature in Kelvin
22g CO2
CO2 Molar Mass = 44g/mol
C = 12g/mol
O = 16g/mol
P = 0.8210atm
V = 50L
PV = nRT
0.8210 x 50 = 8.314 x 0.5 x T
41.05 = 4.157T
T = 41.05/4.157
T = 9.875K
<span>H2PCH3 + H2O <-----> H3PCH3+ + OH-</span>
