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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. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    CO competes with oxygen at the heme binding site. Hemoglobin's binding affinity for CO is 250 times greater than its affinity for oxygen, [ 69 ] [ 70 ] Since carbon monoxide is a colorless, odorless and tasteless gas, and poses a potentially fatal threat, carbon monoxide detectors have become commercially available to warn of dangerous levels ...

  4. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    Globin synthesis takes place in the ribosomes which are located within the cytosol. 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.

  5. 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.

  6. Hemoprotein - Wikipedia

    en.wikipedia.org/wiki/Hemoprotein

    Heme is bound to the protein either covalently or noncovalently or both. [2] The heme consists of iron cation bound at the center of the conjugate base of the porphyrin, as well as other ligands attached to the "axial sites" of the iron. The porphyrin ring is a planar dianionic, tetradentate ligand.

  7. Aminolevulinic acid synthase - Wikipedia

    en.wikipedia.org/wiki/Aminolevulinic_acid_synthase

    Aminolevulinic acid synthase (ALA synthase, ALAS, or delta-aminolevulinic acid synthase) is an enzyme (EC 2.3.1.37) that catalyzes the synthesis of δ-aminolevulinic acid (ALA) the first common precursor in the biosynthesis of all tetrapyrroles such as hemes, cobalamins and chlorophylls. [1]

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  9. Heme B - Wikipedia

    en.wikipedia.org/wiki/Heme_B

    Heme B or haem B (also known as protoheme IX) is the most abundant heme. [1] Hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. The COX-1 and COX-2 enzymes (cyclooxygenase) of recent fame, also contain heme B at one of two active sites.