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  2. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    Heme synthesis in the cytoplasm and mitochondrion. The enzymatic process that produces heme is properly called porphyrin synthesis, as all the intermediates are tetrapyrroles that are chemically classified as porphyrins. The process is highly conserved across biology.

  3. 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]

  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. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    This process also produces one molecule of carbon monoxide for every molecule of heme degraded. [80] Heme degradation is the only natural source of carbon monoxide in the human body, and is responsible for the normal blood levels of carbon monoxide in people breathing normal air. [81] The other major final product of heme degradation is ...

  6. Porphyrin - Wikipedia

    en.wikipedia.org/wiki/Porphyrin

    A common synthesis for porphyrins is the Rothemund reaction, first reported in 1936, [12] [13] which is also the basis for more recent methods described by Adler and Longo. [14] The general scheme is a condensation and oxidation process starting with pyrrole and an aldehyde.

  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. Hemoprotein - Wikipedia

    en.wikipedia.org/wiki/Hemoprotein

    A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. [1] They are a very large class of metalloproteins . The heme group confers functionality, which can include oxygen carrying , oxygen reduction, electron transfer, and other processes.

  9. Delta-aminolevulinic acid dehydratase - Wikipedia

    en.wikipedia.org/wiki/Delta-aminolevulinic_acid...

    It therefore catalyzes the condensation of 2 molecules of 5-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). This reaction is the first common step in the biosynthesis of all biological tetrapyrroles. Zinc is essential for enzymatic activity.