enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  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...

    These molecules of oxygen bind to the globin chain of the heme prosthetic group. [1] [2] When hemoglobin has no bound oxygen, nor bound carbon dioxide, it has the unbound conformation (shape). The binding of the first oxygen molecule induces change in the shape of the hemoglobin that increases its ability to bind to the other three oxygen ...

  6. Cyanide poisoning - Wikipedia

    en.wikipedia.org/wiki/Cyanide_poisoning

    Cyanide binds avidly to methemoglobin, forming cyanmethemoglobin, thus releasing cyanide from cytochrome oxidase. [38] Treatment with nitrites is not innocuous as methemoglobin cannot carry oxygen, and severe methemoglobinemia may need to be treated in turn with methylene blue. [note 1] Thiosulfate

  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. 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.

  9. Carboxyhemoglobin - Wikipedia

    en.wikipedia.org/wiki/Carboxyhemoglobin

    The average red blood cell contains 250 million hemoglobin molecules. [7] Hemoglobin contains a globin protein unit with four prosthetic heme groups (hence the name heme-o-globin); each heme is capable of reversibly binding with one gaseous molecule (oxygen, carbon monoxide, cyanide, etc.), [8] therefore a typical red blood cell may carry up to one billion gas molecules.