Transferrin, a mechanism for iron release.

作者: Jean-Michel El Hage Chahine , Rowchanak Pakdaman

DOI: 10.1111/J.1432-1033.1995.1102G.X

关键词:

摘要: Iron release from transferrin has been investigated in mildly acidic and media the presence of formate, acetate citrate. It occurs first N-terminal iron-binding site (N-site) holoprotein. is independent nature concentration competing ligands controlled by a slow proton transfer; second-order rate constant k1 = (7.4 +/- 0.5) x 10(4) M-1 s-1 which can be attributed to rate-limiting gain protein ligand subsequent fast decarbonation N-site. loss C-terminal (C-site) slower than that N-site two pathways. The favoured below pH 4 does not involve formation an intermediate ternary complex. proton-triggered binding site; k3 (2.25 0.05) s-1. second pathway above involves mixed protein-ligand iron takes place through protonation complex depends on ligand. faster citrate acetate; k4 (1.75 0.10) 10(3) for (85 5) acetate. All these phenomena possibly describe changes conformation sites.

参考文章(43)
D. N. Hague, Dynamics of Substitution at Metal Ions Molecular biology, biochemistry, and biophysics. ,vol. 24, pp. 84- 106 ,(1977) , 10.1007/978-3-642-81117-3_3
Robert M. Smith, Arthur Earl Martell, Critical Stability Constants ,(2011)
George Winston Bates, Michael R. Schlabach, The reaction of ferric salts with transferrin. Journal of Biological Chemistry. ,vol. 248, pp. 3228- 3232 ,(1973) , 10.1016/S0021-9258(19)44032-5
George W. Bates, Joachim Wernicke, The Kinetics and Mechanism of Iron (III) Exchange between Chelates and Transferrin Journal of Biological Chemistry. ,vol. 246, pp. 3679- 3685 ,(1971) , 10.1016/S0021-9258(18)62181-7
P. Aisen, A. Leibman, J. Zweier, Stoichiometric and site characteristics of the binding of iron to human transferrin. Journal of Biological Chemistry. ,vol. 253, pp. 1930- 1937 ,(1978) , 10.1016/S0021-9258(19)62337-9
R E Cowart, N Kojima, G W Bates, The exchange of Fe3+ between acetohydroxamic acid and transferrin. Spectrophotometric evidence for a mixed ligand complex. Journal of Biological Chemistry. ,vol. 257, pp. 7560- 7565 ,(1982) , 10.1016/S0021-9258(18)34416-8