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:
In this experiment, different solutions are made by mixing water with different colors and amounts of food coloring. Students should notice that once the water and colors are mixed together, the liquid looks the same throughout. It is a solution—a homogeneous mixture
Explanation:
I don't know sorry I really need point
The question is incomplete but i will try to offer as much help as i can.
Answer:
See explanation
Explanation:
The electron was discovered by J.J Thompson. His model of the atom was called the plum-pudding model of the atom.
He discovered that cathode rays being negatively charged particles were deflected by a magnet in just the same way as moving, negative electrically charged particles.
Similarly, in an electric field, they are deflected towards the positive plate of the electrostatic field which shows that they are negatively charged.
