Crichton

R. Crichton, Inorganic Biochemistry of Iron Metabolism, Ellis Horwood, Kernel Hempstead, 1991, 212 pp. 

Peters, S.W., Jones, B.M., Jacobs, A. and Wagstaff, M. (1985). Free iron and lipid peroxidation in the plasma of patients with iron overload. In Proteins of Iron Storage and Transport (eds. G. Spik, J. Montreuil, R.R. Crichton and J. Mazurier) pp. 321-324. Elsevier Science Publishers, New York. 

Clinical Consequences. 2e Robert Crichton Copyright 2001 John Wiley Sons Ltd ISBNs 0-471-49223-X (Hardback) 0-470-84579-1 (Electronic)... 

Inorganic biochemistry of iron metabolism from molecular mechanisms to clinical consequences / Robert Crichton with the collaboration of Johan Boelart. .. [et aZ.].—2nd ed. p. cm. 

Figure 1.1 Some redox potentials (in volts) of iron and copper enzymes and chelates at pH 7 relative to the standard hydrogen electrode. From Crichton and Pierre, 2001. Reproduced by permission of Kluwer academic publishers.

Figure l.4 The structural variety of trinuclear ferric hydroxo complexes, Fe3(OH)f i, that could form from Fe2(OH)24+ at low pH. Iron atoms are indicated as full circles, OH as open circles. The arrow indicates a transition from dinuclears to trinuclears (p = 2 to p = 3), which is realistic as an early step in the growth of polynuclears. (From Crichton, 1991.)... 

Figure 1.5 The variation of precipitation times with molar ratios of a = HCO3 / Fe(III) for 0.6 M iron(III) perchlorate solutions, t is the somewhat arbitrarily defined time elapsed before a Tyndall effect is observed. (From Crichton, 1991.)...

Figure 5.14 The transferrin to cell cycle. (From Crichton, 1991.)...

Ferritins have been found in a wide range of species, and sequence data - some, as in the first ever sequence of horse spleen apoferritin (Heusterspreute and Crichton, 1981) determined by direct methods, but many now by DNa sequencing 1, have been deposited for more than 70 ferritins. They vary in length from 154-185 residues per subunit. Some ferritins have N-terminal extensions which lie on the outside of the assembled shell and target the ferritin to a specific destination such as plastids in plants and yolk sac in snails (Andrews etah, 1992 Lobreaux etah, 1992). For example, pea ferritin is synthesized with an N-terminal extension of 75 residues, which is missing from the mature protein. The first part of this extension is a chloroplast-targetting sequence of 47 residues, which is lost on entry into the plastid. The second part, an extension peptide, is lost prior to assembly of the... 

Figure 6.13 Electron micrograph of human spleen ferritin viewed at a magnification of x 170 000 after negative staining with uranyl acetate. Both the darkly coloured iron-rich cores and the clear-coloured protein shells are clearly visible. (From Crichton, 1991.)...

Iron oxidized by ferritin must be at or near the outer surface of the apoferritin molecule, since iron appears to be exchanged between ferritin molecules, as shown by Mossbauer spectroscopy (Bauminger et ah, 1991a,b) and by the observation that iron oxidized by ferritin can be taken up directly by apotransferrin (Bakker and Boyer, 1986 Jin and Crichton, 1987). 

---