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:
lithium
Explanation:
this is because lithium has a valency of 1 and oxygen has a valency of 2 thereby exchanging valency to create Li²0
The charge of this atom would be -2
1) As can be seen from any 1H NMR chemical shift ppm tables, hydrogens which have δ values from 2ppm to 2.3ppm are hydrogens from carbon which is bonded to a carbonyl group. From this, we can conclude that our hydrogens belong to the type, but from 2 different alkyl groups because of 2 different signals.
2) So, one alkyl group is CH3 and second one can be CH or CH2.
3) If we know that ratio between two types of hydrogens is 3:2, it can be concluded that second alkyl group is CH2.
4) Finally, we don't have any other signals and it indicates that part of the compound which continues on CH2 is exactly the same as the first part.
The ratio remains the same, 3:2 ie 6:4
