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  2. Iron in biology - Wikipedia

    en.wikipedia.org/wiki/Iron_in_biology

    The most commonly known and studied bioinorganic iron compounds (biological iron molecules) are the heme proteins: examples are hemoglobin, myoglobin, and cytochrome P450. [1] These compounds participate in transporting gases, building enzymes, and transferring electrons. [5] Metalloproteins are a group of proteins with metal ion cofactors.

  3. Metalloprotein - Wikipedia

    en.wikipedia.org/wiki/Metalloprotein

    Metalloenzymes all have one feature in common, namely that the metal ion is bound to the protein with one labile coordination site. As with all enzymes, the shape of the active site is crucial. The metal ion is usually located in a pocket whose shape fits the substrate. The metal ion catalyzes reactions that are difficult to achieve in organic ...

  4. Iron-binding proteins - Wikipedia

    en.wikipedia.org/wiki/Iron-binding_proteins

    Iron-binding proteins are carrier proteins and metalloproteins that are important in iron metabolism [1] and the immune response. [2] [3] Iron is required for life.Iron-dependent enzymes catalyze a variety of biochemical reactions and can be divided into three broad classes depending on the structure of their active site: non-heme mono-iron, non-heme diiron , or heme centers. [4]

  5. Ferritin - Wikipedia

    en.wikipedia.org/wiki/Ferritin

    Ferritin genes are highly conserved between species. All vertebrate ferritin genes have three introns and four exons. [8] In human ferritin, introns are present between amino acid residues 14 and 15, 34 and 35, and 82 and 83; in addition, there are one to two hundred untranslated bases at either end of the combined exons. [9]

  6. Transferrin - Wikipedia

    en.wikipedia.org/wiki/Transferrin

    The protein is composed of alpha helices and beta sheets that form two domains. [18] The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. [12] The amino acids which bind the iron ion to the transferrin are identical for both lobes; two tyrosines, one histidine, and one aspartic acid.

  7. Siderophore - Wikipedia

    en.wikipedia.org/wiki/Siderophore

    The most effective siderophores are those that have three bidentate ligands per molecule, forming a hexadentate complex and causing a smaller entropic change than that caused by chelating a single ferric ion with separate ligands. [16] Fe 3+ is a strong Lewis acid, preferring strong Lewis bases such as anionic or neutral oxygen atoms to ...

  8. ‘Elevated Levels’ of Heavy Metals Found in Popular Protein ...

    www.aol.com/scientists-just-found-lead-cadmium...

    A new Clean Label Project report suggests some protein powders contain heavy metals lead and cadmium. See which ones are safe here, plus what an expert advises. ‘Elevated Levels’ of Heavy ...

  9. Iron–sulfur protein - Wikipedia

    en.wikipedia.org/wiki/Iron–sulfur_protein

    Proteins are also known to contain [Fe 3 S 4] centres, which feature one iron less than the more common [Fe 4 S 4] cores. Three sulfide ions bridge two iron ions each, while the fourth sulfide bridges three iron ions. Their formal oxidation states may vary from [Fe 3 S 4] + (all-Fe 3+ form) to [Fe 3 S 4] 2− (all-Fe 2+ form).

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