Iron protein electron transport

Fe Cytochrome oxidase reduction of oxygen to water Cytochrome P-450 0-insertion from O2, and detoxification Cytochromes b and c electron transport in respiration and photosynthesis Cytochrome f photosynthetic electron transport Ferredoxin electron transport in photosynthesis and nitrogen fixation Iron-sulfur proteins electron transport in respiration and photosynthesis Nitrate and nitrite reductases reduction to ammonium... 

Carter C. W., Jr. (1977). New stereochemical analogies between iron-sulfur electron transport proteins./. Biol. Chem. 252, 7802-7811. 

Ruthenium, osmium, and rheitium complexes have been used to define electron-transfer rates over defined distances and pathways see Iron Heme Proteins Electron Transport, Long-range Electron Transfer in Biology) They can be attached to external His residues by displacement of its... 

Biomineralization Iron Heme Proteins Dioxygen Transport Storage Iron Heme Proteins Electron Transport Iron Heme Proteins, Mono- Dioxygenases Iron Heme Proteins, Peroxidases, Catalases Catalase-peroxidases Iron Inorganic Coordination Chemistry Iron Proteins with Dinuclear Active Sites Iron Proteins with Mononuclear Active Sites Iron-Sulfur Proteins Iron Transport Siderophores Metal Ion Toxicity. 

Copper Enzymes in Denitrification Iron Heme Proteins Dioxygen Transport Storage bon Heme Proteins Electron Transport Iron Heme Proteins, Mono- ... 

Copper Proteins with Type 1 Sites Iron Heme Proteins Electron Transport Long-range Electron Transfer in Biology Manganese The Oxygen-evolving Complex Models. 

Perhaps the best-characterized example of this mechanism involves the synthesis of heme cofactors and their subsequent incorporation into various hemoproteins (see Iron Heme Proteins Electron Transport). Succinctly, enzyme-catalyzed reactions convert either succinyl-CoA or glutamate into 5-ammolevulinic acid. This molecule is further converted through a series of intermediates to form protoporphyrin IX, the metal-ffee cofactor, into which Fe is inserted by ferrochelatase. Analogous reactions are required for the synthesis of other tetrapyrrole macrocycles such as the cobalamins (see Cobalt Bu Enzymes Coenzymes), various types of chlorophylls, and the methanogen coenzyme F430 (containing Co, Mg, or Ni, respectively). Co- and Mg-chelatases have been described for insertion of these metals into the appropriate tetrapyrrolic ring structures. ... 

Calcium-binding Proteins Copper Enzymes in Denitrification Copper Proteins with Type 1 Sites Copper Proteins with Type 2 Sites Iron Heme Proteins Electron Transport Iron-Sulfin Proteins Metal-mediated Protein Modification Metallochaperones Metal Ion Homeostasis Molybdenum MPT-containing Enzymes Nickel Enzymes Cofactors, Nitrogenase Catalysis Assembly Zinc Enzymes. 

Most known multiheme cytochromes and enzymes belong to the family of cytochromes c (see Iron Heme Proteins Electron Transport), which contain Fe-protoporphyrin IX covalently attached to the polypeptide chain by two thioether bonds, formed by addition of two cysteinyl residues to the vinyl side-chains of the porphyrin ring. The two cysteines form a characteristic amino acid sequence motif CXXCH, usually indicative of heme c ligation, and where the histidine is the axial fifth ligand to the iron. For some cytochromes (see Section 2), the number of residues between the two cysteines can be three or four. The heme redox potentials in cytochromes c cover a wide range and are tuned by several factors, usually dominated by the type of axial ligation and the extent of solvent exposure of the heme. ... 

---