Solution Speciation of the Dinuclear ZrIV-Substituted Keggin Polyoxometalate [{α-PW11O39Zr(μ-OH)(H2O)}2]8-and Its Reactivity towards DNA-Model Phosphodiester Hydrolysis

2014 ◽  
Vol 2014 (31) ◽  
pp. 5276-5284 ◽  
Author(s):  
Thi Kim Nga Luong ◽  
Gregory Absillis ◽  
Pavletta Shestakova ◽  
Tatjana N. Parac-Vogt
2018 ◽  
Vol 7 (1) ◽  
pp. 13-20
Author(s):  
Romain Canioni ◽  
Emmanuel Cadot ◽  
R. John Errington ◽  
Nathalie Leclerc-Laronze ◽  
Catherine Roch-Marchal

Viruses ◽  
2018 ◽  
Vol 10 (5) ◽  
pp. 265 ◽  
Author(s):  
Xiaoli Wang ◽  
Jiao Wang ◽  
Wenmei Zhang ◽  
Boye Li ◽  
Ying Zhu ◽  
...  

2021 ◽  
Author(s):  
János P. Mészáros ◽  
Veronika F. S. Pape ◽  
Gergely Szakács ◽  
Gábor Németi ◽  
Márk Dénes ◽  
...  

A series of half-sandwich polypyridyl complexes was synthesized and compared focusing on structural, cytotoxic and aqueous solution behaviour. The formula of the synthesized complexes is [M(arene)(N,N)Cl]Cl, where M: Ru or...


2020 ◽  
Author(s):  
Shreya Ghosh ◽  
Anam Ejaz ◽  
Lucas Repeta ◽  
Stewart Shuman

Abstract Pseudomonas putida MPE exemplifies a novel clade of manganese-dependent single-strand DNA endonuclease within the binuclear metallophosphoesterase superfamily. MPE is encoded within a widely conserved DNA repair operon. Via structure-guided mutagenesis, we identify His113 and His81 as essential for DNA nuclease activity, albeit inessential for hydrolysis of bis-p-nitrophenylphosphate. We propose that His113 contacts the scissile phosphodiester and serves as a general acid catalyst to expel the OH leaving group of the product strand. We find that MPE cleaves the 3′ and 5′ single-strands of tailed duplex DNAs and that MPE can sense and incise duplexes at sites of short mismatch bulges and opposite a nick. We show that MPE is an ambidextrous phosphodiesterase capable of hydrolyzing the ssDNA backbone in either orientation to generate a mixture of 3′-OH and 3′-PO4 cleavage products. The directionality of phosphodiester hydrolysis is dictated by the orientation of the water nucleophile vis-à-vis the OH leaving group, which must be near apical for the reaction to proceed. We propose that the MPE active site and metal-bound water nucleophile are invariant and the enzyme can bind the ssDNA productively in opposite orientations.


2014 ◽  
Vol 118 (9) ◽  
pp. 2396-2404 ◽  
Author(s):  
G. De Luca ◽  
F. Bisignano ◽  
A. Figoli ◽  
F. Galiano ◽  
E. Furia ◽  
...  

Polyhedron ◽  
2014 ◽  
Vol 67 ◽  
pp. 242-252 ◽  
Author(s):  
Éva A. Enyedy ◽  
Gabriella M. Bognár ◽  
Nóra V. Nagy ◽  
Tamás Jakusch ◽  
Tamás Kiss ◽  
...  

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