Hemoglobin's role is central to respiratory physiology, as it not only carries oxygen but also plays a part in transporting carbon dioxide back to the lungs. Structurally, hemoglobin is made of four subunits, each capable of binding one oxygen molecule. This multi-unit configuration allows for cooperative binding. When one oxygen molecule binds, the hemoglobin changes shape slightly, making it easier for additional oxygen molecules to attach.
- Each hemoglobin can carry four oxygen molecules at its full capacity.
- Binding is influenced by several factors including the pH and concentration of carbon dioxide.
- This cooperative nature ensures swift oxygen attachment in the lungs and rapid release in tissues requiring oxygen.
Moreover, hemoglobin's versatility ensures that not only oxygen, but carbon dioxide and protons are transported, playing a role in pH regulation through the buffering system.