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

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. Sternbergb and T. L. Blundellc*

aBiomolecular 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

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Positively charged groups of proteins, such as the α-amino terminus, [epsilon]-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[link]). [\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]

Figure 12.1.5.7 | top | pdf |

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








































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