- Hemoglobin-0.mp3
- Hemoglobin-0.mp4
- Hemoglobin-I.mp3
- Hemoglobin-I.mp4
- Hemoglobin-II.mp3
- Hemoglobin-II.mp4
- Hemoglobin-III.mp3
- Hemoglobin-III.mp4
- Hemoglobin-Reprise.mp3
- Hemoglobin-intro.mp3
[Intro]
[Instrumental, Guitar Solo]
Crucial protein…
No what I mean
I can’t breathe
What’s beneath?
[Verse 1]
Hemoglobin
Red from iron
Bound to oxygen
I can breath again
[Chorus]
My heart bleeds
(For you)
My mind concedes
(It’s true)
[Bridge]
Allosteric regulation
(O2 distribution)
pH balance
(A delicate dance)
[Verse 2]
Hemoglobin
Let the oxygen in
Find out about
Letting CO2 out
[Chorus]
My heart bleeds
(For you)
My mind concedes
(It’s true)
[Bridge]
Allosteric regulation
(O2 distribution)
pH balance
(A delicate dance)
[Chorus]
My heart bleeds
(For you)
My mind concedes
(It’s true)
[Outro]
My heart bleeds
(My mind concedes)
A SCIENCE NOTE
Hemoglobin is a crucial protein in red blood cells responsible for transporting oxygen and carbon dioxide throughout the body. Here’s a detailed look at its functions:
1. Oxygen Transport
- Binding Oxygen in the Lungs:
- Hemoglobin binds to oxygen molecules in the lungs, where oxygen concentration is high.
- Each hemoglobin molecule contains four heme groups, each with an iron atom that binds one oxygen molecule, allowing each hemoglobin molecule to carry up to four oxygen molecules.
- Delivering Oxygen to Tissues:
- In tissues where oxygen levels are low, hemoglobin releases oxygen, which diffuses into cells for use in cellular respiration to produce energy.
2. Carbon Dioxide Transport
- Binding Carbon Dioxide in Tissues:
- Hemoglobin helps transport carbon dioxide (a waste product of cellular respiration) from tissues back to the lungs for exhalation.
- About 20-25% of carbon dioxide binds directly to hemoglobin to form carbaminohemoglobin.
- The rest is transported as bicarbonate ions in the blood.
- Releasing Carbon Dioxide in the Lungs:
- In the lungs, hemoglobin releases carbon dioxide, which is exhaled.
3. Buffering pH
- Hemoglobin plays a role in maintaining the blood’s pH balance by binding or releasing hydrogen ions (H⁺) in response to changes in blood acidity.
- This helps keep the blood pH within the narrow range necessary for proper cellular function.
4. Adaptation to Oxygen Needs
- Allosteric Regulation:
- Hemoglobin changes its shape (conformation) depending on oxygen levels, carbon dioxide levels, and pH.
- This allows hemoglobin to efficiently pick up oxygen in the lungs and release it in tissues where it’s needed.
- Bohr Effect:
- In tissues with high carbon dioxide levels or low pH, hemoglobin’s affinity for oxygen decreases, facilitating oxygen release.
Key Features
- Structure:
- Hemoglobin is a tetramer, consisting of four polypeptide chains (two alpha and two beta chains).
- Each chain contains a heme group with an iron atom that binds oxygen.
- Color:
- Hemoglobin gives blood its red color due to the iron in the heme group, which turns bright red when bound to oxygen.
Clinical Relevance
- Anemia: A deficiency in hemoglobin can result in insufficient oxygen delivery, leading to fatigue and weakness.
- Carbon Monoxide Poisoning: Hemoglobin binds carbon monoxide with much greater affinity than oxygen, blocking oxygen transport.
- Sickle Cell Disease: A genetic mutation in hemoglobin causes red blood cells to deform, impairing oxygen delivery and causing complications.