The bioinorganic chemistry of iron in oxygenases and supramolecular assemblies.
The bioinorganic chemistry of iron is central to life processes. Organisms must recruit iron from their environment, control iron storage and trafficking within cells, assemble the complex, iron-containing redox cofactors of metalloproteins, and manage a myriad of biochemical transformations by those enzymes. The coordination chemistry and the variable oxidation states of iron provide the essential mechanistic machinery of this metabolism. Our current understanding of several aspects of the chemistry of iron in biology are discussed with an emphasis on the oxygen activation and transfer reactions mediated by heme and nonheme iron proteins and the interactions of amphiphilic iron siderophores with lipid membranes.
Groves
John T
JT
Department of Chemistry, Princeton University, Princeton, NJ 08544, USA. jtgroves@princeton.edu
D015393:Chemistry, Bioinorganic / Q000379:methods*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism; D006420:Hemeproteins / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D008958:Models, Molecular; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism; D011487:Protein Conformation
D006420:Hemeproteins; D003577:Cytochrome P-450 Enzyme System; D007501:Iron; D010088:Oxidoreductases; D010100:Oxygen