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  2. Cyanide poisoning - Wikipedia

    en.wikipedia.org/wiki/Cyanide_poisoning

    Cyanide is a potent cytochrome c oxidase (COX, a.k.a. Complex IV) inhibitor, causing asphyxiation of cells. As such, cyanide poisoning is a form of histotoxic hypoxia, because it interferes with the ability of cells to take or use oxygen via oxidative phosphorylation. [ 25 ]: 1475. Specifically, cyanide binds to the heme a3-CuB binuclear center ...

  3. Cyanide - Wikipedia

    en.wikipedia.org/wiki/Cyanide

    The cyanide anion is an inhibitor of the enzyme cytochrome c oxidase (also known as aa 3), the fourth complex of the electron transport chain found in the inner membrane of the mitochondria of eukaryotic cells. It attaches to the iron within this protein. The binding of cyanide to this enzyme prevents transport of electrons from cytochrome c to

  4. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    This positive cooperative binding is achieved through steric conformational changes of the hemoglobin protein complex as discussed above; i.e., when one subunit protein in hemoglobin becomes oxygenated, a conformational or structural change in the whole complex is initiated, causing the other subunits to gain an increased affinity for oxygen.

  5. Methemoglobin - Wikipedia

    en.wikipedia.org/wiki/Methemoglobin

    It works by converting hemoglobin to methemoglobin, which allows for the binding of cyanide (CN –) anions by ferric (Fe 3+) cations and the formation of cyanomethemoglobin. The immediate goal of forming this cyanide adduct is to prevent the binding of free cyanide to the cytochrome a 3 group in cytochrome c oxidase. [8]

  6. 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.

  7. Oxygen–hemoglobin dissociation curve - Wikipedia

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

    In its simplest form, the oxyhemoglobin dissociation curve describes the relation between the partial pressure of oxygen (x axis) and the oxygen saturation (y axis). Hemoglobin's affinity for oxygen increases as successive molecules of oxygen bind. More molecules bind as the oxygen partial pressure increases until the maximum amount that can be ...

  8. Blood agent - Wikipedia

    en.wikipedia.org/wiki/Blood_agent

    v. t. e. A blood agent is a toxic chemical agent that affects the body by being absorbed into the blood. [ 1 ] Blood agents are fast-acting, potentially lethal poisons that typically manifest at room temperature as volatile colorless gases with a faint odor. [ 1 ] They are either cyanide - or arsenic -based.

  9. Cytochrome c oxidase - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_c_oxidase

    OPM protein. 2dyr. Membranome. 257. The enzyme cytochrome c oxidase or Complex IV (was EC 1.9.3.1, now reclassified as a translocase EC 7.1.1.9) is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes. [ 1 ] It is the last enzyme in the respiratory electron transport chain of cells located in the ...