For example, the atomic mass of an oxygen atom is 16.00 amu; that means the molar mass of an oxygen atom is 16.00 g/mol. Further, if you have 16.00 grams of oxygen atoms, you know from the definition of a mole that your sample contains 6.022 x 10^23 oxygen atoms.
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:
it can tell and show what pathogen is in you as well what type and mutation so then your body can fight back and remember the genetic dna so then you will be immune in some way.
Explanation:
The correct answer is (C. zirconium - 93.
