Electrostatic binding of heavy-atom anions

Carvin, D.; Islam, S. A.; Sternberg, M. J. E.; Blundell, T. L.

doi:10.1107/97809553602060000679

International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

pdf | chapter contents | chapter index | related articles

International Tables for Crystallography (2006). Vol. F. ch. 12.1, p. 253 | 1 | 2 |

Section 12.1.5.4. Electrostatic binding of heavy-atom anions

D. Carvin,^a S. A. Islam,^b M. J. E. Sternberg^b and T. L. Blundell^c ^*

^a Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Field, London WC2A 3PX, England,^bInstitute of Cancer Research, 44 Lincoln's Inn Fields, London WC2A 3PX, England, and ^cDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge, CB2 1GA, England
Correspondence e-mail: tom@cryst.bioc.cam.ac.uk

12.1.5.4. Electrostatic binding of heavy-atom anions

| top | pdf |

Positively charged groups of proteins, such as the α-amino terminus, ɛ-amino of lysine, guanidinium of arginine and imadazolium of histidine, may form ion pairs with heavy-atom anionic complexes. For example, $[\hbox{HgI}_{4}^{2-}]$ and $[\hbox{HgI}_{3}^{-}]$ can bind through electrostatic interactions. Anionic metal cyanide complexes tend to be more resistant to substitution and consequently interact electrostatically on most occasions. For example, $[\hbox{Pt(CN)}_{4}^{2-}]$ binds at several sites involving lysine or arginine residues in proteins (Fig. 12.1.5.7). $[\hbox{Pt(CN)}_{4}^{2-}]$ and $[\hbox{Au(CN)}_{2}^{-}]$ can act as inhibitors by binding at coenzyme phosphate sites.

Figure 12.1.5.7 | top | pdf |

The binding of $[\hbox{Pt(CN)}_{4}^{2-}]$ to aldose dehydrogenase (8ADH).

References

International Tables for Crystallography (2006). Vol. F. ch. 12.1, p. 253