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  2. Human iron metabolism - Wikipedia

    en.wikipedia.org/wiki/Human_iron_metabolism

    The human body needs iron for oxygen transport. Oxygen (O 2) is required for the functioning and survival of nearly all cell types. Oxygen is transported from the lungs to the rest of the body bound to the heme group of hemoglobin in red blood cells. In muscles cells, iron binds oxygen to myoglobin, which regulates its release.

  3. Iron in biology - Wikipedia

    en.wikipedia.org/wiki/Iron_in_biology

    Of this, about 2.5 g is contained in the hemoglobin needed to carry oxygen through the blood (around 0.5 mg of iron per mL of blood), [25] and most of the rest (approximately 2 grams in adult men, and somewhat less in women of childbearing age) is contained in ferritin complexes that are present in all cells, but most common in bone marrow ...

  4. Blood - Wikipedia

    en.wikipedia.org/wiki/Blood

    Hemoglobin has an oxygen binding capacity between 1.36 and 1.40 ml O 2 per gram hemoglobin, [23] which increases the total blood oxygen capacity seventyfold, [24] compared to if oxygen solely were carried by its solubility of 0.03 ml O 2 per liter blood per mm Hg partial pressure of oxygen (about 100 mm Hg in arteries).

  5. Oxygen–hemoglobin dissociation curve - Wikipedia

    en.wikipedia.org/wiki/Oxygen–hemoglobin...

    Hemoglobin (Hb) is the primary vehicle for transporting oxygen in the blood. Each hemoglobin molecule has the capacity to carry four oxygen molecules. These molecules of oxygen bind to the globin chain of the heme prosthetic group. [1] When hemoglobin has no bound oxygen, nor bound carbon dioxide, it has the unbound conformation (shape). The ...

  6. Cellular respiration - Wikipedia

    en.wikipedia.org/wiki/Cellular_respiration

    In the presence of oxygen, when acetyl-CoA is produced, the molecule then enters the citric acid cycle (Krebs cycle) inside the mitochondrial matrix, and is oxidized to CO 2 while at the same time reducing NAD to NADH. NADH can be used by the electron transport chain to create further ATP as part of oxidative phosphorylation. To fully oxidize ...

  7. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    Two globin chains that have heme groups combine to form hemoglobin. One of the chains is an alpha chain and the other is a non-alpha chain. Non-alpha chain nature in hemoglobin molecules varies due to different variables. Fetuses have a non-alpha chain called gamma and after birth it is then called beta. The beta chain will pair with the alpha ...

  8. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    Hemoglobin has an oxygen-binding capacity of 1.34 mL of O 2 per gram, [6] which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. [7] The mammalian hemoglobin molecule can bind and transport up to four oxygen molecules. [8] Hemoglobin also transports other gases.

  9. Hemocyanin - Wikipedia

    en.wikipedia.org/wiki/Hemocyanin

    Most hemocyanins bind with oxygen non-cooperatively and are roughly one-fourth as efficient as hemoglobin at transporting oxygen per amount of blood. Hemoglobin binds oxygen cooperatively due to steric conformation changes in the protein complex , which increases hemoglobin's affinity for oxygen when partially oxygenated.

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