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:
D
Explanation:
I believe the answer is D.
Answer:
The differemt isotopes that differ in atomic mass
Explanation:
<span>Answers are:
-4 for C in CH4, because carbon has greater electronegativity than hydrogen and he attracts shared electrons.
</span><span>+4 for C in CO2, because carbon has smaller electronegativity than oxygen.
</span><span>+1 for H in both CH4 and H2O, because hydrogen has amaller electronegativity than both carbon and oxygen.
</span>
Tomato juice or acid rain
