Oxygen catalyzed mobilization of iron from ferritin by iron(III) chelate ligands. 2011

Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
State University of New York at Potsdam, Department of Chemistry, Potsdam, New York, USA. bouabdf@potsdam.edu

Tridentate chelate ligands of 2,6-bis[hydroxy(methyl)amino]-1,3,5-triazine family rapidly release iron from human recombinant ferritin in the presence of oxygen. The reaction is inhibited by superoxide dismutase, catalase, mannitol and urea. Suggested reaction mechanism involves reduction of the ferritin iron core by superoxide anion, diffusion of iron(II) cations outside the ferritin shell, and regeneration of superoxide anions through oxidation of iron(II) chelate complexes with molecular oxygen.

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D007502 Iron Chelating Agents Organic chemicals that form two or more coordination links with an iron ion. Once coordination has occurred, the complex formed is called a chelate. The iron-binding porphyrin group of hemoglobin is an example of a metal chelate found in biological systems. Iron Chelates,Agents, Iron Chelating,Chelates, Iron,Chelating Agents, Iron
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008024 Ligands A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) Ligand
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010100 Oxygen An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration. Dioxygen,Oxygen-16,Oxygen 16
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002374 Catalase An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA. Catalase A,Catalase T,Manganese Catalase,Mn Catalase
D002384 Catalysis The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction. Catalyses
D005293 Ferritins Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types. Basic Isoferritin,Ferritin,Isoferritin,Isoferritin, Basic

Related Publications

Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
June 2010, Metallomics : integrated biometal science,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
January 1987, The Biochemical journal,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
December 1980, Journal of inorganic biochemistry,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
February 1968, Biochemistry,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
September 1980, Biochimica et biophysica acta,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
September 1981, Biochimica et biophysica acta,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
March 1991, Journal of biochemistry,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
January 2018, Metallomics : integrated biometal science,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
November 2006, The EMBO journal,
Fadi Bou-Abdallah, and Justin McNally, and Xing Xin Liu, and Artem Melman
August 1987, Biochemical pharmacology,
Copied contents to your clipboard!