scholarly journals Dinuclear metal(ii)-acetato complexes based on bicompartmental 4-chlorophenolate: syntheses, structures, magnetic properties, DNA interactions and phosphodiester hydrolysis

2016 ◽  
Vol 45 (32) ◽  
pp. 12933-12950 ◽  
Author(s):  
Salah S. Massoud ◽  
Catherine C. Ledet ◽  
Thomas Junk ◽  
Simone Bosch ◽  
Peter Comba ◽  
...  
Keyword(s):  
Magnetic Properties ◽  
Dna Interactions ◽  
Phosphodiester Hydrolysis ◽  
Hydrolysis Of

Dinuclear Ni(ii)-, Cu(ii)-, Zn(ii)- and Mn(ii)-acetato complexes have been used in the cleavage of DNA and the hydrolysis of BDNPP.

scholarly journals Pseudomonas putida MPE, a manganese-dependent endonuclease of the binuclear metallophosphoesterase superfamily, incises single-strand DNA in two orientations to yield a mixture of 3′-PO4 and 3′-OH termini

2020 ◽  
Author(s):  
Shreya Ghosh ◽  
Anam Ejaz ◽  
Lucas Repeta ◽  
Stewart Shuman
Keyword(s):  
Pseudomonas Putida ◽  
Bound Water ◽  
Acid Catalyst ◽  
Nuclease Activity ◽  
Single Strand ◽  
Dna Endonuclease ◽  
Dependent Endonuclease ◽  
Leaving Group ◽  
Phosphodiester Hydrolysis ◽  
Hydrolysis Of

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.

Di and tetranuclear Cu(II) complexes with simple 2-aminoethylpyridine: Magnetic properties, phosphodiester hydrolysis, DNA binding/cleavage, cytotoxicity and catecholase activity

Polyhedron ◽  
2019 ◽  
Vol 164 ◽  
pp. 202-218 ◽  
Author(s):  
Popuri Sureshbabu ◽  
Qazi Mohammad Junaid ◽  
C. Upadhyay ◽  
W. Victoria ◽  
Vidhyapriya Pitchavel ◽  
...  
Keyword(s):  
Magnetic Properties ◽  
Dna Binding ◽  
Catecholase Activity ◽  
Phosphodiester Hydrolysis
Sign in / Sign up

Export Citation Format

Share Document