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  2. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    Heme D is the site for oxygen reduction to water of many types of bacteria at low oxygen tension. [24] Heme S is related to heme B by having a formyl group at position 2 in place of the 2-vinyl group. Heme S is found in the hemoglobin of a few species of marine worms.

  3. Carboxyhemoglobin - Wikipedia

    en.wikipedia.org/wiki/Carboxyhemoglobin

    The most extensively studied pathway is the metabolism of heme by heme oxygenase which occurs throughout the body with significant activity in the spleen to facilitate hemoglobin breakdown during erythrocyte recycling. Therefore heme can both carry carbon monoxide in the case of carboxyhemoglobin, or, undergo enzymatic catabolism to generate ...

  4. File:Heme o structure.svg - Wikipedia

    en.wikipedia.org/wiki/File:Heme_o_structure.svg

    The following other wikis use this file: Usage on azb.wikipedia.org هم او; Usage on de.wikipedia.org Häme (Stoffgruppe) Protohäm-IX-Farnesyltransferase

  5. 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 ...

  6. Table of standard reduction potentials for half-reactions ...

    en.wikipedia.org/wiki/Table_of_standard...

    "Oxidation-reduction potentials, absorbance bands and molar absorbance of compounds used in biochemical studies" (PDF). Fasman GD, Editor. 1: 122– 130. Alberty, Robert A. (1998). "Calculation of standard transformed formation properties of biochemical reactants and standard apparent reduction potentials of half reactions".

  7. Oxygen–hemoglobin dissociation curve - Wikipedia

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

    The oxygen–hemoglobin dissociation curve, also called the oxyhemoglobin dissociation curve or oxygen dissociation curve (ODC), is a curve that plots the proportion of hemoglobin in its saturated (oxygen-laden) form on the vertical axis against the prevailing oxygen tension on the horizontal axis.

  8. Heme A - Wikipedia

    en.wikipedia.org/wiki/Heme_a

    Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule and is produced naturally by many organisms. Heme A, often appears a dichroic green/red when in solution, is a structural relative of heme B, a component of hemoglobin, the red pigment in blood.

  9. File:Heme a.svg - Wikipedia

    en.wikipedia.org/wiki/File:Heme_a.svg

    The following other wikis use this file: Usage on bs.wikipedia.org Hem; Usage on de.wikipedia.org Häme (Stoffgruppe) Usage on es.wikipedia.org Hemo