Question

How is hemoglobin's affinity for oxygen affected by the presence or absence of oxygen?Rank hemoglobin molecules with the described conditions from most likely to bind oxygen molecules to most likely to release oxygen molecules. (For help approaching this problem, open Hint 1.)

Answer 1

Explanation:

Hemoglobin is a blood hemoprotein, with a molecular mass of 64,000 g / mol (64 kDa), of a characteristic red color, which transports the dioxygen (commonly called oxygen), O2, from the respiratory organs to the tissues, the dioxide of carbon, CO2, from the tissues to the lungs that eliminate it and also participates in the regulation of blood pH, in vertebrates and some invertebrates.

Hemoglobin is a quaternary structure protein, which consists of four subunits. This protein is part of the hemoprotein family, since it has 1 heme group in each subunit

Hemoglobin is a tetrameric protein, which consists of four polypeptide chains with different primary structures. ... Each hemoglobin polypeptide chain is attached to a heme group to form a subunit. The four subunits of hemoglobin in its quaternary structure form a tetrahedron.

Answer 2

Completed Question

How is hemoglobin's affinity for oxygen affected by the presence or absence of oxygen? Rank hemoglobin molecules with the described conditions from most likely to bind oxygen molecules to most likely to release oxygen molecules. (For help approaching this problem, open Hint 1.) View Available Hint(s) Reset 1 bound O2 Po, = 40 mm Hg 3 bound O2, Po, = 40 mm Hg 1 bound O2, Po, 100 mm Hg 3 bound O2, Po, = 100 mm Hg most likely to bind oxygen molecules most likely to release oxygen molecules Submit

Answer:

Basically the percentage saturation of Oxygen is determined by the partial pressure PO2 of oxygen available.Thus haemoglobin  binds with more oxygen molecules at high partial pressure of oxygen thus  well saturated with oxygen.That is all the 8 oxygen atoms combined the iron atoms of  the haem group.

However at at low partial pressure a few oxygen molecules binds with haemoglobin,and thus less saturated. The differences in oxygen partial pressure explains why at high oxygen partial pressure the dissociation curve shift to the left,  to hold oxygen This is important in the lungs for oxygen  trapping from lung tissues.And at low partial pressure  when to  deliver  oxygen the Sigmoid curve shift to the right so  that oxygen is  release

Based on this  pressure fluctuations and oxygen affinity.

Most likely

3 bound O2, Po, = 100 mm Hg-

it will be faster for  3 -oxygen molecules to bind because of high pressure. Once  the first oxygen molecule binds with the haem groups to distort it,  and weaken it,other 2 oxygen molecules will bind faster, aiding saturation.and most  likely bonding

1 bound O2, Po, 100 mm Hg

-although only one oxygen molecule at 100 mmHg, it will take a lot of time for the first oxygen atom to distort the haem bonds to bind with haemoglobin.

1 bound O2 Po, = 40 mm Hg -

at lower pressure  Hb binding is reduced therefore difficult for oxygen to bind with Hb

3 bound O2, Po, = 40 mm Hg-

it will take a longer time for the oxygen molecules to bind with the Heame group, at low pressure because the oxygen molecules will queue after the first oxygen atom which wil find it difficult to bond with the heame group so the least likely.

Least likely

Explanation: