title: How are hydrogen bonds modified by metal binding?
abstract: We have used density functional theory calculations to investigate how the hydrogen-bond strength is modified when a ligand is bound to a metal using over 60 model systems involving six metals and eight ligands frequently encountered in metalloproteins. We study how the hydrogen-bond geometry and energy vary with the nature of metal, the oxidation state, the coordination number, the ligand involved in the hydrogen bond, other first-sphere ligands, and different hydrogen-bond probe molecules. The results show that, in general, the hydrogen-bond strength is increased for neutral ligands and decreased for negatively charged ligands. The size of the effect is mainly determined by the net charge of the metal complex, and all effects are typically decreased when the model is solvated. In water solution, the hydrogen-bond strength can increase by up to 37 kJ/mol for neutral ligands, and that of negatively charged ligands can increase (for complexes with a negative net charge) or decrease (for positively charged complexes). If the net charge of the complex does not change, there is normally little difference between different metals or different types of complexes. The only exception is observed for sulphur-containing ligands (Met and Cys) and if the ligand is redox-active (e.g. high-valence Fe-O complexes).
authors.affiliation: Department of Theoretical Chemistry, Chemical Centre, Lund University, P.O. Box 124, 221 00 Lund, Sweden.
authors.forename: Charlotte
authors.initials: C
authors.lastname: Husberg
authors.forename: Ulf
authors.initials: U
authors.lastname: Ryde
mesh_terms: D006860:Hydrogen Bonding; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry*; D008670:Metals / Q000737:chemistry*; D015394:Molecular Structure; D013816:Thermodynamics
chemical_list: D008024:Ligands; D008667:Metalloproteins; D008670:Metals
references.citation: Chembiochem. 2003 May 9;4(5):413-24
references.pmid: 12740813
references.citation: Chem Rev. 2010 Feb 10;110(2):949-1017
references.pmid: 19813749
references.citation: Chem Rev. 2010 Sep 8;110(9):5023-63
references.pmid: 20486691
references.citation: Biophys J. 1999 Nov;77(5):2777-87
references.pmid: 10545376
references.citation: J Biol Inorg Chem. 1999 Feb;4(1):99-110
references.pmid: 10499107
references.citation: J Chem Phys. 2010 Apr 21;132(15):154104
references.pmid: 20423165
references.citation: J Phys Chem B. 2008 Feb 28;112(8):2501-10
references.pmid: 18251539
references.citation: J Am Chem Soc. 2002 Nov 6;124(44):13257-64
references.pmid: 12405854
references.citation: Angew Chem Int Ed Engl. 2011 Jan 10;50(2):352-3
references.pmid: 21132822
references.citation: Phys Rev A Gen Phys. 1988 Sep 15;38(6):3098-3100
references.pmid: 9900728
references.citation: Chemphyschem. 2011 Dec 9;12(17):3421-33
references.pmid: 22113958
references.citation: J Chem Theory Comput. 2011 Jan 11;7(1):88-96
references.pmid: 26606221
references.citation: Chem Rev. 1996 Nov 7;96(7):2239-2314
references.pmid: 11848828
references.citation: Science. 1995 May 26;268(5214):1144-9
references.pmid: 7761829
references.citation: Phys Chem Chem Phys. 2012 Aug 21;14(31):10896-8
references.pmid: 22772777
references.citation: Adv Inorg Biochem. 1988;7:1-36
references.pmid: 2821744
references.citation: J Biol Inorg Chem. 2000 Oct;5(5):565-74
references.pmid: 11085647
references.citation: J Inorg Biochem. 2009 Jul;103(7):1054-60
references.pmid: 19501913
references.citation: J Am Chem Soc. 2011 Apr 6;133(13):4810-8
references.pmid: 21405134
references.citation: J Biol Inorg Chem. 2004 Mar;9(2):203-23
references.pmid: 14727167
references.citation: J Am Chem Soc. 2003 Apr 2;125(13):3980-7
references.pmid: 12656634
references.citation: Phys Rev B Condens Matter. 1988 Jan 15;37(2):785-789
references.pmid: 9944570
references.citation: Phys Rev B Condens Matter. 1986 Jun 15;33(12):8822-8824
references.pmid: 9938299
references.citation: J Chem Theory Comput. 2011 Aug 9;7(8):2427-2438
references.pmid: 21836824
references.citation: Phys Chem Chem Phys. 2006 May 7;8(17):1985-93
references.pmid: 16633685
references.citation: Curr Opin Chem Biol. 2009 Feb;13(1):84-8
references.pmid: 19345605
references.citation: Angew Chem Int Ed Engl. 2010 Dec 27;49(52):10045-7
references.pmid: 21117106
references.citation: J Phys Chem A. 2011 May 5;115(17):4115-34
references.pmid: 21476557
references.citation: J Comput Chem. 2006 Sep;27(12):1398-414
references.pmid: 16802319
references.citation: J Mol Biol. 1988 Oct 20;203(4):1071-95
references.pmid: 3210236
references.citation: Science. 2001 Mar 16;291(5511):2118-20
references.pmid: 11251110
references.citation: Biophys J. 2004 Nov;87(5):3437-47
references.pmid: 15339813
references.citation: Inorg Chem. 2001 May 21;40(11):2509-19
references.pmid: 11350228
references.citation: J Phys Chem A. 2007 Aug 23;111(33):8257-63
references.pmid: 17649987
references.citation: Annu Rev Biophys Biophys Chem. 1990;19:301-32
references.pmid: 2194479
references.citation: Chem Rev. 2005 Aug;105(8):2999-3093
references.pmid: 16092826
references.citation: Protein Sci. 1996 Jul;5(7):1229-39
references.pmid: 8819156
references.citation: Dalton Trans. 2011 Nov 14;40(42):11176-83
references.pmid: 21853206
references.citation: Phys Chem Chem Phys. 2007 Jun 21;9(23):2959-67
references.pmid: 17551619