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  2. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    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] Heme is biosynthesized in both the bone marrow and ...

  3. 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

  4. 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 ...

  5. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    For instance, succinylacetone has been shown to decrease heme concentrations by inhibiting δ-aminolevulinic acid in murine erythroleukemia cells. [20] The primary structure of heme-sequestering peptides, such as HSP1 and HSP2, can be modified to downregulate heme concentrations and reduce proliferation of non-small lung cancer cells.

  6. Hemoprotein - Wikipedia

    en.wikipedia.org/wiki/Hemoprotein

    β-sheet miniproteins [33] Multi-stranded β-sheet peptides [34] Some methodologies attempt to incorporate cofactors into the hemoproteins who typically endure harsh conditions. In order to incorporate a synthetic cofactor, what must first occur is the denaturing of the holoprotein to remove the heme. The apoprotein is then rebuilt with the ...

  7. 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.

  8. Wikipedia : Manual of Style/Chemistry/Structure drawing

    en.wikipedia.org/wiki/Wikipedia:Manual_of_Style/...

    The program can read and write many file formats, other than its proprietary sketch file format (.skc) and can export PNG files. If SVG files are required, it is recommended that structure diagrams be exported as enhanced metafiles (.emf) which can be read by Inkscape and other image editors..

  9. Heme transporter - Wikipedia

    en.wikipedia.org/wiki/Heme_transporter

    Heme is a major source of dietary iron in humans and other mammals, and its synthesis in the body is well understood, but heme pathways are not as well understood. It is likely that heme is tightly regulated for two reasons: the toxic nature of iron in cells, and the lack of a regulated excretory system for excess iron.