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Hemoglobin

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Hemoglobin

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Hemoglobin

He-man-globe
Picmonic
Hemoglobin is a metalloprotein in blood that carries oxygen from the alveolus to all tissues in the body. It is composed of four iron heme subunits that can each individually bind oxygen. These four hemes participate in cooperative binding, which means that when one heme subunit binds oxygen, the others are more likely to bind more oxygen. This gives the oxygen saturation curve its characteristic shape. There are many hemoglobin molecules in red blood cells because the body has high oxygen demands. In areas of high oxygen concentration, the propensity to bind oxygen increases. Such areas include the alveolus, where hemoglobin needs to bind oxygen in order to deliver it to cells. In areas with high carbon dioxide levels, the propensity to bind oxygen decreases, allowing hemoglobin to drop oxygen off in high metabolic areas (because CO2 is a byproduct of metabolism). Additionally, high temperatures and low pH levels reduce oxygen binding. There is a derivative of hemoglobin, myoglobin, which is only found in muscle tissue. It only has one subunit rather than four.
7 KEY FACTS
Hemoglobin Has Four Iron Hemes
He-man-globe with (4) Fork Iron

Hemoglobin is composed of four iron heme subunits that can each individually bind oxygen. These four hemes participate in cooperative binding, which means that when one heme subunit binds oxygen, the others are more likely to bind.

Lots Of Hemoglobin In Red Blood Cells
Lots of He-man-globes in RBC truck

Lots of hemoglobin is needed in red blood cells because of the high oxygen demands of the body.

High O2 Levels Increase O2 Binding
Lots of O2-tanks cause up-arrow He-man-globe binding

High O2 levels increases hemoglobin's binding affinity for oxygen, allowing it to pick up oxygen in areas like the alveolus.

High Temperature Reduces O2 Binding
Hot-flame makes He-man-globe to drop Down-arrow O2-tank

High temperature also reduces oxygen-binding affinity in hemoglobin as part of the physiological response to hyperthermia.

High CO2 Levels Reduce O2 Binding
Many CO2-molecules pushing Down-arrow O2-tanks Off

High carbon dioxide levels reduce hemoglobin's binding affinity for oxygen, allowing it to drop oxygen off at tissues. Because tissues are undergoing cellular metabolism, they produce CO2 as a byproduct and use O2 as an electron acceptor.

Low pH Reduces O2 Binding
Acidic-lemon with Down-arrow dropping O2 tanks

Low pH reduces O2 binding in a condition called acidosis. If respiration levels are low and CO2 is not being exhaled fast enough, blood becomes acidic and O2 binding in hemoglobin is reduced.

Myoglobin Binds Oxygen in Muscle
Mayo-globe held by Muscle-man

Myoglobin is a hemoglobin derivative found only in muscle cells. It has one subunit instead of four.

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