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:
The third one down: "When barium hydroxide is mixed with ammonium chloride, ice crystals form on the outside of the container."
This is because an endothermic reaction [process] takes in more energy than it releases. Therefore because a decrease in energy leads to a decrease in temperature, the ice crystals forming show that it must be a endothermic reaction [process].
Hope this helps! :)
AJ
Answer:
Concept: Chemical Analysis
- Start by taking inventory of the elements that you have
- Make a list, one for the right side and another for the left side
- Then add coefficients to the elements to the right or left side to balance out the equation
Answer:
2
Explanation:
In the equation, Cl is chlorine and there is a number "2" so that the correct answer is 2.
