Nuclearity dependent solvent contribution to the catechol oxidase activity of novel copper(ii) complexes derived from Mannich-base ligand platforms: synthesis, crystal structure and mechanism

2017 ◽  
Vol 41 (16) ◽  
pp. 8586-8597 ◽  
Author(s):  
Ria Sanyal ◽  
Sergey Ketkov ◽  
Suranjana Purkait ◽  
Franz A. Mautner ◽  
Grigory Zhigulin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Oxidase Activity ◽  
Mannich Base ◽  
Kinetic Studies ◽  
Catechol Oxidase ◽  
Catecholase Activity

Solvent-dependent kinetic studies of the catecholase activity of a set of Cu(ii) complexes reveal alcoholysis and hydrolysis as the governing factors for kcat extrema.

Thioether sulfur-bound [Cu2] complexes showing catechol oxidase activity and DNA cleaving behaviour

2019 ◽  
Vol 48 (4) ◽  
pp. 1292-1313 ◽  
Author(s):  
Manisha Das ◽  
Zeenat Afsan ◽  
Dipmalya Basak ◽  
Farukh Arjmand ◽  
Debashis Ray
Keyword(s):  
Oxidase Activity ◽  
Catechol Oxidase ◽  
Dna Molecules ◽  
Dna Cleaving ◽  
Catecholase Activity

Ligand backbone alteration leads to different mechanisms for catecholase activity and order of interaction with DNA molecules.

scholarly journals Impact of Thiocyanate on the Catecholase Activity of Cu(II) and Fe(III) Complexes of 2-((4-(2-Hydroxy-4-Methylbenzyl)Piperazin-1-YL)Methyl)-5-Methylphenol (A Mannich Base)

2018 ◽  
Vol 26 (1) ◽  
pp. 59-73 ◽  
Author(s):  
Ayowole O. Ayeni ◽  
Gareth M. Watkins
Keyword(s):  
Catalytic Activity ◽  
Infrared Spectroscopy ◽  
Metal Complexes ◽  
Turnover Rate ◽  
Mannich Base ◽  
Kinetic Studies ◽  
Spectroscopic Techniques ◽  
Synthetic Route ◽  
Tert Butyl ◽  
Catecholase Activity

Abstract Four metal complexes viz Cu(II) and Fe(III) with or without thiocyanate have been synthesized from a Mannich base prepared by a simple synthetic route. These complexes were characterized by elemental and spectroscopic techniques. Bonding modes of the thiocyanate group with the metal complexes as studied by infrared spectroscopy revealed the presence of bridging N- and S- bonding modes. Detailed kinetic studies of these complexes were carried in the evaluation of their catecholase activity. The Fe(III) complex demonstrated the highest catalytic activity using 3,5-di-tert-butyl catechol (3,5-DTBC) as substrate with a turnover rate (kcat) of 112.32 h−1.

scholarly journals Hydrogen peroxide‐mediated conversion of coproheme to heme b by HemQ—lessons from the first crystal structure and kinetic studies

FEBS Journal ◽  
2016 ◽  
Vol 283 (23) ◽  
pp. 4386-4401 ◽  
Author(s):  
Stefan Hofbauer ◽  
Georg Mlynek ◽  
Lisa Milazzo ◽  
Dominic Pühringer ◽  
Daniel Maresch ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hydrogen Peroxide ◽  
Kinetic Studies

scholarly journals Structure of theMycobacterium tuberculosisd-Alanine:d-Alanine Ligase, a Target of the Antituberculosis Drug d-Cycloserine

2010 ◽  
Vol 55 (1) ◽  
pp. 291-301 ◽  
Author(s):  
John B. Bruning ◽  
Ana C. Murillo ◽  
Ofelia Chacon ◽  
Raúl G. Barletta ◽  
James C. Sacchettini
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Kinetic Studies ◽  
Structural Rearrangement ◽  
Peptidoglycan Biosynthesis ◽  
Binding Cavity ◽  
Binding Pockets ◽  
Loop Regions ◽  
Discrete Domains ◽  
Alanine Dipeptide

ABSTRACTd-Alanine:d-alanine ligase (EC 6.3.2.4; Ddl) catalyzes the ATP-driven ligation of twod-alanine (d-Ala) molecules to form thed-alanyl:d-alanine dipeptide. This molecule is a key building block in peptidoglycan biosynthesis, making Ddl an attractive target for drug development.d-Cycloserine (DCS), an analog ofd-Ala and a prototype Ddl inhibitor, has shown promise for the treatment of tuberculosis. Here, we report the crystal structure ofMycobacterium tuberculosisDdl at a resolution of 2.1 Å. This structure indicates that Ddl is a dimer and consists of three discrete domains; the ligand binding cavity is at the intersection of all three domains and conjoined by several loop regions. TheM. tuberculosisapo Ddl structure shows a novel conformation that has not yet been observed in Ddl enzymes from other species. The nucleotide andd-alanine binding pockets are flexible, requiring significant structural rearrangement of the bordering regions for entry and binding of both ATP andd-Ala molecules. Solution affinity and kinetic studies showed that DCS interacts with Ddl in a manner similar to that observed ford-Ala. Each ligand binds to two binding sites that have significant differences in affinity, with the first binding site exhibiting high affinity. DCS inhibits the enzyme, with a 50% inhibitory concentration (IC50) of 0.37 mM under standard assay conditions, implicating a preferential and weak inhibition at the second, lower-affinity binding site. Moreover, DCS binding is tighter at higher ATP concentrations. The crystal structure illustrates potential drugable sites that may result in the development of more-effective Ddl inhibitors.

Azide-mediated unusual in situ transformation of Mannich base to Schiff-Mannich base and isolation of their Cu(II) complexes: crystal structure, theoretical inspection and anticancer activities

2021 ◽  
Author(s):  
Debasis Das ◽  
Somali Mukherjee ◽  
Sili Hansda ◽  
Sudeshna Nandi ◽  
Krishnendu Acharya ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mannich Base ◽  
Coupling Reactions ◽  
Anticancer Activities ◽  
Pendant Arms

A new “end-off” compartmental Mannich ligand (HL1) namely 3-((bis(2-methoxyethyl)amino)methyl)-5-bromo-2-hydroxybenzaldehyde containing two methoxyethyl pendant arms and one-CHO functionality has been synthesized through conventional C-C and C-N coupling reactions. On treatment with...

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