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The Irving-Williams Series refers to the relative stabilities of complexes formed by transition metals. In 1953 Harry Irving and Robert Williams observed that the stability of complexes formed by divalent first-row transition metal ions generally increase across the period to a maximum stability at copper : Mn(II) < Fe(II) < Co(II) < Ni(II) < Cu(II) > Zn(II). [1]
Explanation
[edit]Three explanations are frequently used to explain the series:
- The ionic radius is expected to decrease regularly from Mn(II) to Zn(II). This is the normal periodic trend and would account for the general increase in stability.
- The Crystal Field Stabilization Energy (CFSE) increases from zero for Mn(II) to a maximum at Ni(II). This makes the complexes increasingly stable. CFSE for Zn(II) is zero.
- Although the CFSE of Cu(II) is less than that of Ni(II), octahedral Cu(II) complexes are subject to the Jahn-Teller effect, which affords octahedral Cu(II) complexes additional stability.
However, none of the above explanations can satisfactorily explain the success of the Irving–Williams series in predicting the relative stabilities of transition metal complexes. A recent study of metal-thiolate complexes indicates that an interplay between covalent and electrostatic contributions in metal-ligand binding energies might result in Irving–Williams series.[2]
Some actual CFSE values for octahedral complexes of first-row transition metals (∆oct) are 0.4Δ (4 Dq) for iron, 0.8Δ (8 Dq) for cobalt and 1.2Δ (12 Dq) for nickel. When the stability constants are quantitatively adjusted for these values they follow the trend that is predicted, in the absence of crystal field effects, between manganese and zinc.[clarification needed] This was an important factor contributing to the acceptance of crystal field theory, the first theory to successfully account for the thermodynamic, spectroscopic and magnetic properties of complexes of the transition metal ions and precursor to ligand field theory.[3][relevant?]
Biological relevance
[edit]The Irving-Williams series is a dominant factor affecting the biodistribution of transition metals.[4].
- Copper is highest in the the Irving-Williams series, which means that Cu(II) will tend to outcompete other divalent transition metals for metal-binding residues in metalloproteins.
- Selective delivery of metals to proteins is necessary to obtain functional protein. Cells achieve specificity by use of compartmentalization and metal chaperones, which allow cells to balance binding affinities with metal availability.
- Pumps can enrich or deplete the cell cytoplasm of particular metal ions, or alternatively affect the concentration of free ions within vesicles or other intracellular compartments.[4]
- ...metal chaperons, on the other hand...
See also
[edit]References
[edit]- ^ Irving, H. M. N. H.; Williams, R. J. P. (1953). "The stability of transition-metal complexes". J. Chem. Soc.: 3192–3210. doi:10.1039/JR9530003192.
- ^ Gorelsky, S. I.; Basumallick, L.; Vura-Weis, J.; Sarangi, R.; Hodgson, K. O.; Hedman, B.; Fujisawa, K.; Solomon, E. I. (2005). "Spectroscopic and DFT Investigation of M{HB(3,5-iPr2pz)3}(SC6F5) (M = Mn, Fe, Co, Ni, Cu, and Zn) Model Complexes: Periodic Trends in Metal-thiolate Bonding". Inorg. Chem. 44 (14): 4947–4960. doi:10.1021/ic050371m. PMC 2593087. PMID 15998022.
{{cite journal}}: CS1 maint: date and year (link) - ^ Orgel, L. E. (1966). An introduction to transition-metal chemistry: ligand-field theory (2nd ed.). London: Methuen.
- ^ a b Kraatz, ed. by Heinz-Bernhard; Metzler-Nolte, Nils (2006). Concepts and models in bioinorganic chemistry. Weinheim: Wiley-VCH-Verl. pp. 11–14. ISBN 3-527-31305-2.
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