Steric Bulkiness-Dependent Structural Diversity in Nickel(II) Complexes of N-Heterocyclic Carbenes: Synthesis and Structural Characterization of Tetra-, Penta-, and Hexacoordinate Nickel Complexes

2009 ◽  
Vol 28 (5) ◽  
pp. 1336-1349 ◽  
Author(s):  
Xiaoming Zhang ◽  
Bin Liu ◽  
Ailing Liu ◽  
Weilong Xie ◽  
Wanzhi Chen

2008 ◽  
Vol 47 (23) ◽  
pp. 11367-11375 ◽  
Author(s):  
Stephen M. Mansell ◽  
Christopher A. Russell ◽  
Duncan F. Wass


Author(s):  
Liam A. Wilson ◽  
Esmée G. Knaven ◽  
Marc T. Morris ◽  
Marcelo Monteiro Pedroso ◽  
Christopher J. Schofield ◽  
...  

The structural diversity in metallo-β-lactamases (MBLs), especially in the vicinity of the active site, has been a major hurdle in the development of clinically effective inhibitors. Representatives from three variants of the B3 MBL subclass, containing either the canonical HHH/DHH active site motif (present in the majority of MBLs in this subclass) or the QHH/DHH (B3-Q) or HRH/DQK (B3-RQK) variations were reported previously. Here, we describe the structure and kinetic properties of the first example (SIE-1) of a fourth variant containing the EHH/DHH active site motif (B3-E). SIE-1 was identified in the hexachlorocyclohexane-degrading bacterium Sphingobium indicum , and kinetic analyses demonstrate that although it is active against a wide range of antibiotics its efficiency is lower than that of other B3 MBLs, but with improved efficiency towards cephalosporins relative to other β-lactam substrates. The overall fold of SIE-1 is characteristic of the MBLs; the notable variation is observed in the Zn1 site due to the replacement of the canonical His116 by a glutamate. The unusual preference of SIE-1 for cephalosporins and its occurrence in a widespread environmental organism suggests scope for increased MBL-mediated β-lactam resistance. It is thus relevant to include SIE-1 into MBL inhibitor design studies to widen the therapeutic scope of much needed anti-resistance drugs.





2015 ◽  
Vol 34 (7) ◽  
pp. 1228-1237 ◽  
Author(s):  
Zehua Yang ◽  
Delong Liu ◽  
Yangang Liu ◽  
Masashi Sugiya ◽  
Tsuneo Imamoto ◽  
...  


ChemInform ◽  
2010 ◽  
Vol 33 (28) ◽  
pp. no-no
Author(s):  
Andreas A. Danopoulos ◽  
Scott Winston ◽  
Thomas Gelbrich ◽  
Michael B. Hursthouse ◽  
Robert P. Tooze


2017 ◽  
Vol 13 ◽  
pp. 1145-1167 ◽  
Author(s):  
Serge Pérez ◽  
Daniele de Sanctis

Synchrotron radiation is the most versatile way to explore biological materials in different states: monocrystalline, polycrystalline, solution, colloids and multiscale architectures. Steady improvements in instrumentation have made synchrotrons the most flexible intense X-ray source. The wide range of applications of synchrotron radiation is commensurate with the structural diversity and complexity of the molecules and macromolecules that form the collection of substrates investigated by glycoscience. The present review illustrates how synchrotron-based experiments have contributed to our understanding in the field of structural glycobiology. Structural characterization of protein–carbohydrate interactions of the families of most glycan-interacting proteins (including glycosyl transferases and hydrolases, lectins, antibodies and GAG-binding proteins) are presented. Examples concerned with glycolipids and colloids are also covered as well as some dealing with the structures and multiscale architectures of polysaccharides. Insights into the kinetics of catalytic events observed in the crystalline state are also presented as well as some aspects of structure determination of protein in solution.



2004 ◽  
Vol 2004 (16) ◽  
pp. 3305-3309 ◽  
Author(s):  
Beatriz Royo ◽  
Eberhardt Herdtweck ◽  
Carlos C. Romão


Polyhedron ◽  
2014 ◽  
Vol 67 ◽  
pp. 490-494 ◽  
Author(s):  
Yu-Long Li ◽  
Bin Xie ◽  
Li-Ke Zou ◽  
Xiao Lin ◽  
Yi Yang ◽  
...  


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