Oxygen and carbon monoxide
Oxygen and carbon dioxide are the two chemicals that bind with hemoglobin in the blood. Oxygen binds to hemoglobin in the lungs for transport around the body, while carbon dioxide binds to hemoglobin in the tissues for removal from the body.
Mostly oxygen.
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Carbon dioxide and BPG bind to amino acids located on hemoglobin. Oxygen molecules bind to the iron molecules located in the heme. Each hemoglobin molecule can carry up to four oxygen molecules, one on each of the four iron molecules. Nitric oxide can also bind to hemoglobin when either oxygen or carbon dioxide are bound to the hemoglobin.
Up to 4.
Hemoglobin is a complex protein with iron groups inside it that bind to oxygen.
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Haemoglobin combines with four molecules of oxygen.
Oxygen has two binding sites in a hemoglobin molecule: one on each of the two alpha-beta dimers. This allows each hemoglobin molecule to bind and carry up to four oxygen molecules.
Hemoglobin cooperativity is a process where the binding of one oxygen molecule to a hemoglobin molecule makes it easier for other oxygen molecules to bind. This means that as more oxygen molecules bind to hemoglobin, the affinity for oxygen increases, allowing hemoglobin to efficiently transport oxygen in the bloodstream.
Carbon monoxide binds to hemoglobin with a higher affinity than oxygen, forming carboxyhemoglobin. This can displace oxygen from hemoglobin, reducing the blood's ability to transport oxygen to tissues, which can lead to serious health consequences.
The cooperativity of hemoglobin refers to how its binding of one oxygen molecule affects its ability to bind more oxygen molecules. When one oxygen molecule binds to hemoglobin, it changes the shape of the protein, making it easier for more oxygen molecules to bind. This makes hemoglobin more efficient at picking up oxygen in the lungs and releasing it to tissues that need it.