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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. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    Hemoglobin A (HbA) is the most common adult form of hemoglobin and exists as a tetramer containing two alpha subunits and two beta subunits (α2β2). [3] Each subunit contains a heme group that diatomic oxygen (O 2) molecules can bind to. [5]

  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. 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. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    The name hemoglobin (or haemoglobin) is derived from the words heme (or haem) and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme group. Each heme group contains one iron atom, that can bind one oxygen molecule through ion-induced dipole forces.

  7. Hemoprotein - Wikipedia

    en.wikipedia.org/wiki/Hemoprotein

    A model of the Fe-protoporphyrin IX subunit of the Heme B cofactor. Because of their diverse biological functions and widespread abundance, hemeproteins are among the most studied biomolecules. [4] Data on heme protein structure and function has been aggregated into The Heme Protein Database (HPD), a secondary database to the Protein Data Bank. [5]

  8. Heme C - Wikipedia

    en.wikipedia.org/wiki/Heme_C

    The redox potential for cytochrome c can also be "fine-tuned" by small changes in protein structure and solvent interaction. [4] The number of heme C units bound to a holoprotein is highly variable. For vertebrate cells one heme C per protein is the rule but for bacteria this number is often 2, 4, 5, 6 or even 16 heme C groups per holoprotein.

  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