Aresearcher has introduced molecules of human myoglobin and human hemoglobin into a solution containing oxygen. which of the following statements is true of human hemoglobin and myoglobin?

(Complete questions below).

ANSWER

→When introduced into an oxygen-containing solution, a single molecule of human myoglobin will bind to more oxygen molecules than a human hemoglobin  molecule will.

Explanation:

Myoglobin(MB) and haemoglobin (HB) are oxygen  binding pigments in   mammals while Hb transports oxygen and other gases in the blood streams,Myoglobin   stores maximum oxygen in the muscles. Thus this explains while it is possible to seize breath   with no effects for few seconds.The oxygen storing capacity  of myoglobin made it a higher binding oxygen pigments than haemoglobin. Hb does not store oxygen  but transports it  in the body.

Structurally,.Heamoglobin is made up of  4-Heme group; while myoglobin has 1 Heme group.The strong affinity and storage capacity for oxygen  is due to non- bonding of distal HIistidine group (His 64) with iron atom.(iron ii) which gives enough flexibility for interactive reactions of Histidine  with oxygen for  maximum oxygen binding and storage,(the proximal histindine group(His-63) is  bonded  directly to the iron atom therefore no flexibity for bonding and stroge with oxygen..

Therefore 1 molecule of MB will  bind to more oxygen molecules(MB02) , than 1 Hb molecule.,(Hb08) even at low concentration.

Complete Question.

A researcher has introduced molecules of human myoglobin and human hemoglobin into a solution containing oxygen. Which of the following statements is true of human hemoglobin and myoglobin?

Because myoglobin does not interact with oxygen molecules, only human hemoglobin will bind to oxygen molecules in this solution.

When introduced into an oxygen-containing solution, a single molecule of human myoglobin will bind to more oxygen molecules than a human hemoglobin molecule will.

When introduced into an oxygen-containing solution, human hemoglobin will bind oxygen molecules more tightly than human myoglobin.

Compared to human hemoglobin, human myoglobin will likely bind to oxygen molecules more quickly when introduced into an oxygen-containing solution.

When introduced into an oxygen-containing solution, human myoglobin and hemoglobin will behave similarly and will bind to the same number of oxygen molecules (with the same affinity).

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