10.1021/jp4041937.s001
Lei Zhou
Lei
Zhou
Shenhui Li
Shenhui
Li
Yongchao Su
Yongchao
Su
Xianfeng Yi
Xianfeng
Yi
Anmin Zheng
Anmin
Zheng
Feng Deng
Feng
Deng
Interaction between Histidine and Zn(II) Metal Ions
over a Wide pH as Revealed by Solid-State NMR Spectroscopy and DFT
Calculations
American Chemical Society
2016
N δ1
N ε2 sites
pH 3.5
biprotonated histidine
pH range
Wide pH
13 C
signal transduction
zinc ion
heteronuclear correlation NMR experiments
NMR parameters
14. 2 D homo
enzymes catalysis
Zn
histidine molecules
benchmark values
DFT CalculationsThe interactions
1 H
deprotonated N δ1 sites
15 N chemical shifts
pH increases
binding
complex
metal species
NMR techniques
acidic pH
2016-02-19 02:28:37
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Interaction_between_Histidine_and_Zn_II_Metal_Ions_over_a_Wide_pH_as_Revealed_by_Solid_State_NMR_Spectroscopy_and_DFT_Calculations/2392087
The interactions between histidine
and metal species play essential
roles in a wide range of important biological processes including
enzymes catalysis and signal transduction. In this work, solid-state
NMR techniques were employed to determine the interaction between
histidine and Zn(II) from pH 3.5 to 14. 2D homo- and heteronuclear
correlation NMR experiments were utilized to extract the <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N chemical shifts in various
histidine–Zn(II) binding complexes. Several histidine–Zn(II)
binding models were proposed on the basis of experimental results
as well as DFT theoretical calculations. No direct interaction could
be found between biprotonated histidine and Zn(II) at acidic pH. At
pH 7.5, one zinc ion could be hexa-coordinated with two histidine
molecules on C′, N<sub>α</sub> and deprotonated N<sub>δ1</sub> sites. As the pH increases to 11–14, both of
the N<sub>δ1</sub> and N<sub>ε2</sub> sites could be deprotonated
as acceptors to be bound to either Zn(II) or water. All of these findings
give a comprehensive set of benchmark values for NMR parameters and
structural geometries in variable histidine–Zn(II) binding
complexes over a wide pH range and might provide insights into the
structure–property relationship of histidine–metal complexes
in biological metalloproteins.