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  2. Methemoglobin - Wikipedia

    en.wikipedia.org/wiki/Methemoglobin

    Methemoglobin cannot bind oxygen, which means it cannot carry oxygen to tissues. It is bluish chocolate-brown in color. It is bluish chocolate-brown in color. In human blood a trace amount of methemoglobin is normally produced spontaneously, but when present in excess the blood becomes abnormally dark bluish brown.

  3. Methemoglobinemia - Wikipedia

    en.wikipedia.org/wiki/Methemoglobinemia

    The binding of oxygen to methemoglobin results in an increased affinity for oxygen in the remaining heme sites that are in ferrous state within the same tetrameric hemoglobin unit. [17] This leads to an overall reduced ability of the red blood cell to release oxygen to tissues, with the associated oxygen–hemoglobin dissociation curve ...

  4. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    The iron ion may be either in the ferrous Fe 2+ or in the ferric Fe 3+ state, but ferrihemoglobin (methemoglobin) (Fe 3+) cannot bind oxygen. [50] In binding, oxygen temporarily and reversibly oxidizes (Fe 2+) to (Fe 3+) while oxygen temporarily turns into the superoxide ion, thus iron must

  5. Oxygen–hemoglobin dissociation curve - Wikipedia

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

    This causes a leftward shift in the oxygen hemoglobin dissociation curve, as any residual heme with oxygenated ferrous iron (+2 state) is unable to unload its bound oxygen into tissues (because 3+ iron impairs hemoglobin's cooperativity), thereby increasing its affinity with oxygen. However, methemoglobin has increased affinity for cyanide, and ...

  6. Hemoglobinopathy - Wikipedia

    en.wikipedia.org/wiki/Hemoglobinopathy

    Methemoglobinemia is a condition caused by elevated levels of methemoglobin in the blood. Methaemoglobin is a form of hemoglobin that contains the ferric [Fe 3+] form of iron, instead of the ferrous [Fe 2+] form . Methemoglobin cannot bind oxygen, which means it cannot carry oxygen to tissues.

  7. Cytochrome b5 reductase - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_b5_reductase

    In living organisms, because methemoglobin (MetHb) is unable to bind oxygen, it must be reduced to hemoglobin (Hb) through the action of the soluble isoform of cytochrome b5 reductase. Overall, the mechanics of this reaction include electron transfer through oxidation steps, which can be accomplished through a couple of different mechanisms ...

  8. Hypoxia in fish - Wikipedia

    en.wikipedia.org/wiki/Hypoxia_in_fish

    Oxygen diffuses into water from air and therefore the top layer of water in contact with air contains more oxygen. This is true only in stagnant water; in running water all layers are mixed together and oxygen levels are the same throughout the water column. One environment where ASR often takes place is tidepools, particularly at night. [34]

  9. Bohr effect - Wikipedia

    en.wikipedia.org/wiki/Bohr_effect

    The Bohr effect increases the efficiency of oxygen transportation through the blood. After hemoglobin binds to oxygen in the lungs due to the high oxygen concentrations, the Bohr effect facilitates its release in the tissues, particularly those tissues in most need of oxygen. When a tissue's metabolic rate increases, so does its carbon dioxide ...