Answer:
σ -> 2sp²
π -> 2p
Explanation:
The carbon has valence shell 2s 2p, and, both of them make 3 σ bonds and 1 π bond. The π bond only occurs in multiple bonds.
The σ bonds happen at the hybrids orbitals, which are orbitals formed by the association of the pure orbitals (s, p, d, f). The hybridization occurs to make possible to the atom to do the bonds because the electrons need to be isolated in it.
On the other hand, the π bonds only occur at pure orbitals. The subshell s only has 1 orbital, and the subshell p has 3 orbitals. So, because there are 3 σ bonds, it's necessary 3 hybrids orbitals (1 of s + 2 of p).
The σ bonds happen at the orbital 2sp² and the π bond at the 2p pure orbital.
Is by turning a few seconds before
Explanation:
The rate of reaction is the speed at which a chemical reaction takes place, defined as proportional to the increase in the concentration of a product per unit time and to the decrease in the concentration of a reactant per unit time. Reaction rates can vary dramatically.
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:
