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 is: <span>- delta G.
</span>The change in Gibbs free energy (ΔG), at constant temperature and pressure, is: <span>ΔG=ΔH−TΔS.
</span>ΔH<span> is the change in enthalpy.
</span>ΔS is change in entropy.
T is temperature of the system.
When ΔG is negative, a reaction (<span>occurs without the addition of external energy)</span><span> will be spontaneous (</span>exergonic).
Answer:
the tertiary animals the bigger animals that feed on smaller fish and crustaceans. These include predators like sharks, barracuda and tuna snapper. these fish that are commercially fished at unsustainable levels.
Explanation:
Answer:
1. During diffusion, when the concentration of molecules on both sides of a membrane is the same, the molecules will continue to move across the membrane in both directions.
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