Targeting metallo-carbapenemases via modulation of electronic properties of cephalosporins

2014 ◽  
Vol 464 (2) ◽  
pp. 271-279 ◽  
Author(s):  
Hao Yang ◽  
Heather Young ◽  
Sophia Yu ◽  
Larry Sutton ◽  
Michael W. Crowder
Keyword(s):  
Electronic Properties ◽  
Residence Time ◽  
Active Site

We demonstrate that the residence time of intermediates formed in the active site of NDM-1 can be tuned by substituents on cephalosporin scaffolds; compounds that reside for long times in the active site could be inhibitors of metallo-β-lactamases.

The Electronic Properties of a Model Active Site for Blue Copper Proteins as Probed by Stark Spectroscopy

2002 ◽  
Vol 106 (11) ◽  
pp. 3007-3012 ◽  
Author(s):  
Arindam Chowdhury ◽  
Linda A. Peteanu ◽  
Patrick L. Holland ◽  
William B. Tolman
Keyword(s):  
Electronic Properties ◽  
Active Site ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Stark Spectroscopy ◽  
Blue Copper

scholarly journals Coordination and conformational isomers in mononuclear iron complexes with pertinence to the [FeFe] hydrogenase active site

2014 ◽  
Vol 43 (11) ◽  
pp. 4537-4549 ◽  
Author(s):  
Andreas Orthaber ◽  
Michael Karnahl ◽  
Stefanie Tschierlei ◽  
Daniel Streich ◽  
Matthias Stein ◽  
...  
Keyword(s):  
Electronic Properties ◽  
Active Site ◽  
Iron Complexes ◽  
Computational Studies ◽  
Mononuclear Iron ◽  
Conformational Isomers ◽  
Ligand Modification ◽  
Fe Complexes ◽  
Ir Spectroscopic

6 Fe complexes of the type [Fe(X-bdt)(PR2NPh2)(CO)] were prepared and the possibility to tune their electronic properties by ligand modification was demonstrated. IR spectroscopic and computational studies suggest that the compounds exist as a mixture of isomers in solution.

Tuning the electronic properties of Fe2(μ-arenedithiolate)(CO)6−n(PMe3)n (n=0, 2) complexes related to the [Fe–Fe]-hydrogenase active site

2008 ◽  
Vol 11 (8) ◽  
pp. 875-889 ◽  
Author(s):  
Lennart Schwartz ◽  
Pradyumna S. Singh ◽  
Lars Eriksson ◽  
Reiner Lomoth ◽  
Sascha Ott
Keyword(s):  
Electronic Properties ◽  
Active Site

Structure and electronic properties of an asymmetric thiolate-bridged binuclear complex: a model for the active site of acetyl CoA synthase

2003 ◽  
pp. 3012-3013 ◽  
Author(s):  
Qiang Wang ◽  
Alexander J. Blake ◽  
E. Stephen Davies ◽  
Eric J. L. McInnes ◽  
Claire Wilson ◽  
...  
Keyword(s):  
Electronic Properties ◽  
Active Site ◽  
Binuclear Complex ◽  
Acetyl Coa

Living and non-living Ziegler–Natta catalysts: electronic properties of active site

Polymer ◽  
2003 ◽  
Vol 44 (21) ◽  
pp. 6555-6558 ◽  
Author(s):  
Gwanghoon Kwag ◽  
Jung-Goo Lee ◽  
Cheolbeom Bae ◽  
Soo No Lee
Keyword(s):  
Electronic Properties ◽  
Active Site ◽  
Ziegler Natta Catalysts

Molecular orbital analysis of active site of oxidized azurin: Dependency of electronic properties on molecular structure

Polyhedron ◽  
2005 ◽  
Vol 24 (16-17) ◽  
pp. 2665-2670 ◽  
Author(s):  
Tomofumi Shuku ◽  
Kimikazu Sugimori ◽  
Ayumu Sugiyama ◽  
Hidemi Nagao ◽  
Takeshi Sakurai ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Electronic Properties ◽  
Molecular Orbital ◽  
Active Site ◽  
Molecular Orbital Analysis ◽  
Orbital Analysis

Modeling the effect of Zn(II) on the hydrogen transfer in inhibition processes

1992 ◽  
Vol 70 (8) ◽  
pp. 2296-2305 ◽  
Author(s):  
Isabel Rozas ◽  
Gustavo A. Arteca
Keyword(s):  
Electronic Properties ◽  
Active Site ◽  
Nicotinamide Adenine Dinucleotide ◽  
Active Sites ◽  
Hydrogen Transfer ◽  
Computation Time ◽  
Inhibitory Mechanism ◽  
Liver Alcohol Dehydrogenase ◽  
Fast Approach ◽  
Metallic Cation

We present in this work the results of a rather simplified theoretical approach to some of the processes involved in the inhibition of Zn-containing active sites. Our aim is to calibrate a model in which Zn is replaced by Be. The motivation for this strategy is to provide a qualitatively correct, but fast, approach that can be used in the simulation of many inhibitors interacting with a Zn site. The use of Be allows us to retain some of the essential features of the inhibitor–Zn interaction, while involving much less computation time. It should be noted that we are not modeling a Be-containing active site, but processes occurring in a Zn-containing one. We design a scaling transformation that permits us to relate the electronic properties associated with a given Be–ligand distance to the same electronic properties associated with a desired Zn–ligand distance. The results provided by the Be-containing model are comparable to those corresponding to the actual Zn-containing model. One of the processes we are interested in describing here is the effect that the presence of a Zn(II) cation has on the ability of an inhibitor to donate a proton to an acceptor. This process is of importance in the inhibition of Zn-containing enzymes, such as liver alcohol dehydrogenase (LADH). The inhibitory mechanism of LADH seems to involve first the interaction of a ligand with the Zn cation, followed by the transfer of a proton to an acceptor, and finally the binding of the deprotonated ligand to the nicotinamide adenine dinucleotide (NAD+) coenzyme. In this work, we considered the molecule of formaldehydehydrazone as a model of an inhibitor (e.g., pyrazole). This simplified model contains the strict essentials needed to study proton transfer mediated by a metallic cation. We found a parallelism between the roles of the two metals in the H transfer from this model of inhibitor that allows us to make some qualitative predictions for other processes in Zn from the results obtained exclusively in the presence of Be.

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