Competitive coordination aggregation for V-shaped [Co3] and disc-like [Co7] complexes: synthesis, magnetic properties and catechol oxidase activity

2016 ◽  
Vol 45 (34) ◽  
pp. 13576-13589 ◽  
Author(s):  
Tufan Singha Mahapatra ◽  
Dipmalya Basak ◽  
Santanu Chand ◽  
Jeff Lengyel ◽  
Michael Shatruk ◽  
...  
Keyword(s):  
Magnetic Properties ◽  
Oxidase Activity ◽  
Catechol Oxidase ◽  
Competitive Coordination

The synthetic procedures, magnetic properties and catecholase-like activity of a V-shaped [CoII3L4] and planar disc-like [CoII7L6] complexes have been discussed.

Anion coordination selective [Mn3] and [Mn4] assemblies: synthesis, structural diversity, magnetic properties and catechol oxidase activity

2015 ◽  
Vol 44 (26) ◽  
pp. 11741-11754 ◽  
Author(s):  
Moumita Pait ◽  
Michael Shatruk ◽  
Debashis Ray
Keyword(s):  
Magnetic Properties ◽  
Magnetic Property ◽  
Schiff Base ◽  
Schiff Base Ligand ◽  
Structural Diversity ◽  
Manganese Complexes ◽  
Catechol Oxidase ◽  
Oxidation Study ◽  
Anion Coordination ◽  
Catechol Oxidation

The present manuscript reports the detail synthesis, characterization, magnetic property and catechol oxidation study of a family of mixed valent (MnIIMnIII) and trivalent (MnIII) manganese complexes from a Schiff base ligand.

scholarly journals Rate enhancement of the catechol oxidase activity of a series of biomimetic monocopper(ii) complexes by introduction of non-coordinating groups in N-tripodal ligands

2012 ◽  
Vol 36 (9) ◽  
pp. 1828 ◽  
Author(s):  
Ronan Marion ◽  
Nidal M. Saleh ◽  
Nicolas Le Poul ◽  
Didier Floner ◽  
Olivier Lavastre ◽  
...  
Keyword(s):  
Oxidase Activity ◽  
Catechol Oxidase ◽  
Tripodal Ligands ◽  
Rate Enhancement

Catechol oxidase activity of comparable dimanganese and dicopper complexes

2018 ◽  
Vol 47 (43) ◽  
pp. 15555-15564
Author(s):  
Adriana M. Magherusan ◽  
Daniel N. Nelis ◽  
Brendan Twamley ◽  
Aidan R. McDonald
Keyword(s):  
Oxidase Activity ◽  
Catechol Oxidase ◽  
Dicopper Complexes

Dicopper complexes proved to be more reactive catechol oxidase mimics when compared to dimanganese complexes supported by identical ligand frameworks.

Substrate Binding in Catechol Oxidase Activity:  Biomimetic Approach

2002 ◽  
Vol 41 (15) ◽  
pp. 3983-3989 ◽  
Author(s):  
Stéphane Torelli ◽  
Catherine Belle ◽  
Sylvain Hamman ◽  
Jean-Louis Pierre ◽  
Eric Saint-Aman
Keyword(s):  
Oxidase Activity ◽  
Substrate Binding ◽  
Catechol Oxidase ◽  
Biomimetic Approach

scholarly journals The action of o-dihydric phenols in the hydroxylation of p-coumaric acid by a phenolase from leaves of spinach beet (Beta vulgaris L.)

1970 ◽  
Vol 119 (1) ◽  
pp. 89-94 ◽  
Author(s):  
P. F. T. Vaughan ◽  
V. S. Butt
Keyword(s):  
Caffeic Acid ◽  
Beta Vulgaris ◽  
Oxidase Activity ◽  
Maximum Rate ◽  
Specific Activity ◽  
Catechol Oxidase ◽  
Coumaric Acid ◽  
Catalytically Active ◽  
Lag Period ◽  
High Concentrations

1. Under defined conditions, the hydroxylation of p-coumaric acid catalysed by a phenolase from leaves of spinach beet (Beta vulgaris L.) was observed to develop its maximum rate only after a lag period. 2. By decreasing the reaction rate with lower enzyme concentrations or by increasing it with higher concentrations of reductants, the length of the lag period was inversely related to the maximum rate subsequently developed. 3. Low concentrations of caffeic acid or other o-dihydric phenols abolished this lag period. With caffeic acid, the rate of hydroxylation was independent of the reductant employed. 4. Hydroxylation was inhibited by diethyldithiocarbamate, but with low inhibitor concentrations hydroxylation recovered after a lag period. This lag could again be abolished by the addition of high concentrations of caffeic acid or other o-dihydric phenols. 5. Catechol oxidase activity showed no lag period, and did not recover from diethyldithiocarbamate inhibition. 6. The purified enzyme contained 0.17–0.33% copper; preparations with the highest specific activity were found to have the highest copper content. 7. The results are interpreted to suggest that the oxidation of o-dihydric phenols converts the enzymic copper into a species catalytically active in hydroxylation. This may represent the primary function for the catechol oxidase activity of the phenolase complex. The electron donors are concerned mainly, but not entirely, in the reduction of o-quinones produced in this reaction.

Catechol oxidase activity in honey from eastern and south-eastern Anatolia

2003 ◽  
Vol 42 (1-2) ◽  
pp. 25-26
Author(s):  
Hayrullah Yilmaz ◽  
Halis Şakiroǧlu ◽  
Ö.Ïrfan Küfrevioǧlu
Keyword(s):  
Oxidase Activity ◽  
Catechol Oxidase ◽  
Eastern Anatolia ◽  
South Eastern
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