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: 10.99
Explanation: because you take the Cao 13.9 and take CO2 which is 10.99 and it makes 24.8 . Which is CaCO3.
Answer:
<u>Explanation</u>:
<u>Number of molecules for
</u>

Atomic mass of Na + H + C + 3(O) = 22.99 + 1.008 + 12.01 + 3 × 16.00 = 84.00 g/mol



<u>Number of molecules for for
</u>

= Atomic mass of 3(Na) + P + 4(O)
= 3(22.99) + 30.97 + 4(16.00) = 163.94 g/mol


Answer:
Please refer to the attachment for answers.
Explanation:
Please refer to the attachment for explanation
My science text book said that it was either diamond or gold. Gold may not be right, but I am pretty sure diamond is.
Sorry if I got this wrong.