Less Symmetrical Dicopper(II) Complexes as Catechol Oxidase Models-An Adjacent Thioether Group Increases Catecholase Activity

2004 ◽  
Vol 11 (4) ◽  
pp. 1201-1209 ◽  
Author(s):  
Michael Merkel ◽  
Niclas Möller ◽  
Manuel Piacenza ◽  
Stefan Grimme ◽  
Annette Rompel ◽  
...  
Keyword(s):  
Catechol Oxidase ◽  
Catecholase Activity

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.

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.

A mononuclear cobalt(iii) complex and its catecholase activity

2015 ◽  
Vol 39 (1) ◽  
pp. 200-205 ◽  
Author(s):  
Merry Mitra ◽  
Pallepogu Raghavaiah ◽  
Rajarshi Ghosh
Keyword(s):  
Catechol Oxidase ◽  
High Turnover ◽  
Mononuclear Cobalt ◽  
Catecholase Activity ◽  
Oxidase Enzyme

A mononuclear Co(iii) complex mimics the catechol oxidase enzyme with appreciably high turnover numbers in different solvents.

Effect of temperature and ligand protonation on the electronic ground state in Cu(ii) polymers having unusual secondary interactions: a magnetic and catechol oxidase study

2018 ◽  
Vol 47 (45) ◽  
pp. 16102-16118 ◽  
Author(s):  
Sandeepta Saha ◽  
Niladri Biswas ◽  
Ashok Sasmal ◽  
Carlos J. Gómez-García ◽  
Eugenio Garribba ◽  
...  
Keyword(s):  
Ground State ◽  
Electronic Ground State ◽  
Effect Of Temperature ◽  
Catechol Oxidase ◽  
Secondary Interactions ◽  
Catecholase Activity ◽  
Electronic Ground

Two new polymeric Cu(ii) compounds with significant catecholase activity are described.

Monophenolase and catecholase activity of Aspergillus oryzae catechol oxidase: insights from hybrid QM/MM calculations

2020 ◽  
Vol 18 (27) ◽  
pp. 5192-5202
Author(s):  
Hao Jiang ◽  
Wenzhen Lai
Keyword(s):  
Aspergillus Oryzae ◽  
Active Site ◽  
Catechol Oxidase ◽  
Catecholase Activity

Monophenolase and diphenolase activities of the [Cu2O2]2+ active site of Aspergillus oryzae catechol oxidase are revealed by hybrid QM/MM calculations.

Tetranuclear Copper and Mononuclear Nickel Complex of the Schiff Base of (3Z)-3-Hydrazonobutan-2-One Oxime with Different Aromatic Carbonyl Compounds: Synthesis, Single Crystal X-Ray Structure, Catecholase Activity, Phenoxazinone Synthase Activity, Catalytic Study for the Homocoupling of Benzyl Amines

2019 ◽  
Author(s):  
Swaraj Sengupta ◽  
Sahanwaj Khan ◽  
Shyamal K. Chattopadhyay ◽  
Indrani Banerjee ◽  
Tarun K. Panda ◽  
...  
Keyword(s):  
Schiff Base ◽  
Single Crystal ◽  
Copper Complex ◽  
Carbonyl Compounds ◽  
Nickel Complex ◽  
Schiff Base Ligands ◽  
X Ray ◽  
Phenoxazinone Synthase ◽  
Catecholase Activity ◽  
Aromatic Carbonyl Compounds

Synthesis and characterisation of one trinuclear copper complex, ([Cu<sub>3</sub>L<sub>3</sub>O]ClO<sub>4</sub>) (<b>1</b>) and one nickel complex ([Ni(L'H)<sub>2</sub>(dmso)<sub>2</sub>](ClO<sub>4</sub>)<sub>2</sub>) (<b>2</b>) with Schiff base ligands: (3Z)-3-((Z)-(1-(thiophen-2-yl)ethylidene)hydrazono)butan-2-one oxime (LH) and 1-(pyridin-2-yl)ethylidene)hydrazono)butan-2-one oxime (L<sup>'</sup>H). <b>1</b> shows high catecholase activity and has also been tested as a catalyst for the synthesis of benzylimine. <b>2 </b> shows phenoxazinone synthase activity.

Development of a new amperometric biosensor based on polyphenoloxidase and polyethersulphone membrane

2001 ◽  
Vol 73 (12) ◽  
pp. 1993-1999 ◽  
Author(s):  
P. V. Climent ◽  
M. L. M. Serralheiro ◽  
M. J. F. Rebelo
Keyword(s):  
Phenolic Compounds ◽  
Response Time ◽  
Enzyme Immobilization ◽  
Platinum Electrode ◽  
Enzymatic Catalysis ◽  
Amperometric Biosensor ◽  
Catecholase Activity

An amperometric biosensor based on the enzyme polyphenoloxidase (PPO), which makes the bioelectrocatalysis of phenolic compounds, was developed and optimized using cathecol as substrate. Polyethersulphone membranes were used for enzyme immobilization. Polyphenoloxidase oxidizes monophenols (cresolase activity) and diphenols (catecholase activity) into the corresponding o-quinones; the o-quinones formed in the enzymatic catalysis are then reduced back to cathecol at ­200 mV (vs. Ag, AgCl) at a platinum electrode. The polyphenoloxidase immobilized was from commercial origin or extracted from mushrooms. p-Cresol and phenol substrates were also tested. Reproducibility, response time, linearity, sensitivity, and stability of the biosensor were studied.

Evidence for conformational changes in grape catechol oxidase

1972 ◽  
Vol 11 (8) ◽  
pp. 2415-2421 ◽  
Author(s):  
H.R. Lerner ◽  
A.M. Mayer ◽  
E. Harel
Keyword(s):  
Conformational Changes ◽  
Catechol Oxidase
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