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  2. Human iron metabolism - Wikipedia

    en.wikipedia.org/wiki/Human_iron_metabolism

    Iron can be stored in ferritin as ferric iron due to the ferroxidase activity of the ferritin heavy chain. [28] Dysfunctional ferritin may accumulate as hemosiderin, which can be problematic in cases of iron overload. [29] The ferritin storage iron pool is much larger than the labile iron pool, ranging in concentration from 0.7 mM to 3.6 mM. [25]

  3. Ferrochelatase - Wikipedia

    en.wikipedia.org/wiki/Ferrochelatase

    Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX in the heme biosynthesis pathway to form heme B. The enzyme is localized to the matrix-facing side of the inner mitochondrial membrane. Ferrochelatase is the best known member of a family of enzymes that add divalent metal cations to tetrapyrrole structures. [2]

  4. Ferredoxin - Wikipedia

    en.wikipedia.org/wiki/Ferredoxin

    Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.

  5. Iron in biology - Wikipedia

    en.wikipedia.org/wiki/Iron_in_biology

    Iron can be stored in ferritin as ferric iron due to the ferroxidase activity of the ferritin heavy chain. [43] Dysfunctional ferritin may accumulate as hemosiderin, which can be problematic in cases of iron overload. [44] The ferritin storage iron pool is much larger than the labile iron pool, ranging in concentration from 0.7 mM to 3.6 mM. [40]

  6. 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]

  7. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    847 12359 Ensembl ENSG00000121691 ENSMUSG00000027187 UniProt P04040 P24270 RefSeq (mRNA) NM_001752 NM_009804 RefSeq (protein) NP_001743 NP_033934 Location (UCSC) Chr 11: 34.44 – 34.47 Mb Chr 2: 103.28 – 103.32 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals ...

  8. Alcohol dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Alcohol_dehydrogenase

    Clostridium acetobutylicum NADPH- and NADH-dependent butanol dehydrogenases EC 1.1.1.-(genes adh1, bdhA and bdhB), [48] enzymes that have activity using butanol and ethanol as substrates. E. coli adhE, [ 49 ] an iron-dependent enzyme that harbours three different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase (acetylating) EC 1.2 ...

  9. Category:Iron enzymes - Wikipedia

    en.wikipedia.org/wiki/Category:Iron_enzymes

    Pages in category "Iron enzymes" The following 81 pages are in this category, out of 81 total. This list may not reflect recent changes.