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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

    In binding, oxygen temporarily and reversibly oxidizes (Fe 2+) to (Fe 3+) while oxygen temporarily turns into the superoxide ion, thus iron must exist in the +2 oxidation state to bind oxygen. If superoxide ion associated to Fe 3+ is protonated, the hemoglobin iron will remain oxidized and incapable of binding oxygen.

  5. Cytochrome b5 reductase - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_b5_reductase

    Methemoglobin is an oxidized form of hemoglobin attached to a ferric-state iron (Fe3+), which can therefore not carry and deliver oxygen to tissues. [15] The formation of methemoglobin occurs when electrons are not returned to the iron of a normal state hemoglobin, which is not preferred for a functioning organism.

  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. 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 ...

  8. Study finds almost all drinking water contains ‘forever ...

    www.aol.com/study-finds-almost-drinking-water...

    Scientists discover 10 PFAS in tap and bottled water in major UK and Chinese cities ... Study finds almost all drinking water contains ‘forever chemicals’ that do not break down naturally.

  9. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    Binding of oxygen to a heme prosthetic group. Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ HEEM), is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. [1]