scholarly journals Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site

2020 ◽  
Author(s):  
Trixia M. Buscagan ◽  
Kathryn A. Perez ◽  
Ailiena O. Maggiolo ◽  
Douglas C. Rees ◽  
Thomas Spatzal
Keyword(s):  
Structural Characterization ◽  
Active Site

Synthesis and structural characterization of cross-linked histidine–phenol Cu(ii) complexes as cytochrome c oxidase active site models

2007 ◽  
pp. 3252 ◽  
Author(s):  
Kimberly N. White ◽  
Indranil Sen ◽  
Istvan Szundi ◽  
Yakira R. Landaverry ◽  
Lauren E. Bria ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Structural Characterization ◽  
Active Site

Spectroscopic, Redox, and Structural Characterization of the Ni-Labile and Nonlabile Forms of the Acetyl-CoA Synthase Active Site of Carbon Monoxide Dehydrogenase

1998 ◽  
Vol 120 (30) ◽  
pp. 7502-7510 ◽  
Author(s):  
William K. Russell ◽  
Christina M. V. Stålhandske ◽  
Jinqiang Xia ◽  
Robert A. Scott ◽  
Paul A. Lindahl
Keyword(s):  
Carbon Monoxide ◽  
Structural Characterization ◽  
Active Site ◽  
Carbon Monoxide Dehydrogenase ◽  
Acetyl Coa

scholarly journals Enantioseparation, in vitro testing, and structural characterization of triple-binding reactivators of organophosphate-inhibited cholinesterases

2020 ◽  
Vol 477 (15) ◽  
pp. 2771-2790 ◽  
Author(s):  
Nikola Maraković ◽  
Anamarija Knežević ◽  
Igor Rončević ◽  
Xavier Brazzolotto ◽  
Zrinka Kovarik ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proton Transfer ◽  
Structural Characterization ◽  
Active Site ◽  
In Vitro Testing ◽  
Active Site Residues

The enantiomers of racemic 2-hydroxyimino-N-(azidophenylpropyl)acetamide-derived triple-binding oxime reactivators were separated, and tested for inhibition and reactivation of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibited with tabun (GA), cyclosarin (GF), sarin (GB), and VX. Both enzymes showed the greatest affinity toward the methylimidazole derivative (III) of 2-hydroxyimino-N-(azidophenylpropyl)acetamide (I). The crystal structure was determined for the complex of oxime III within human BChE, confirming that all three binding groups interacted with active site residues. In the case of BChE inhibited by GF, oximes I (kr = 207 M−1 min−1) and III (kr = 213 M−1 min−1) showed better reactivation efficiency than the reference oxime 2-PAM. Finally, the key mechanistic steps in the reactivation of GF-inhibited BChE with oxime III were modeled using the PM7R6 method, stressing the importance of proton transfer from Nε of His438 to Oγ of Ser203 for achieving successful reactivation.

scholarly journals Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active Site Glutamic Acid

2021 ◽  
Author(s):  
Liam A. Wilson ◽  
Esmée G. Knaven ◽  
Marc T. Morris ◽  
Marcelo Monteiro Pedroso ◽  
Christopher J. Schofield ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Structural Characterization ◽  
Active Site ◽  
Structural Diversity ◽  
Kinetic Properties ◽  
Design Studies ◽  
Degrading Bacterium ◽  
Active Site Motif ◽  
Wide Range

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.

scholarly journals Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site

2020 ◽  
Author(s):  
Trixia M. Buscagan ◽  
Kathryn A. Perez ◽  
Ailiena O. Maggiolo ◽  
Douglas C. Rees ◽  
Thomas Spatzal
Keyword(s):  
Structural Characterization ◽  
Active Site

Structural Characterization of the GSK-3β Active Site Using Selective and Non-selective ATP-mimetic Inhibitors

2003 ◽  
Vol 333 (2) ◽  
pp. 393-407 ◽  
Author(s):  
J.A. Bertrand ◽  
S. Thieffine ◽  
A. Vulpetti ◽  
C. Cristiani ◽  
B. Valsasina ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Active Site ◽  
Gsk 3Β
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