Structures, Magnetochemistry, Spectroscopy, Theoretical Study, and Catechol Oxidase Activity of Dinuclear and Dimer-of-Dinuclear Mixed-Valence MnIIIMnII Complexes Derived from a Macrocyclic Ligand

2013 ◽  
Vol 52 (13) ◽  
pp. 7732-7746 ◽  
Author(s):  
Arpita Jana ◽  
Núria Aliaga-Alcalde ◽  
Eliseo Ruiz ◽  
Sasankasekhar Mohanta
Keyword(s):  
Oxidase Activity ◽  
Theoretical Study ◽  
Macrocyclic Ligand ◽  
Mixed Valence ◽  
Catechol Oxidase

Dinuclear Copper Complexes with Imidazole Derivative Ligands: A Theoretical Study Related to Catechol Oxidase Activity

2012 ◽  
Vol 116 (28) ◽  
pp. 8038-8044 ◽  
Author(s):  
Ana Martínez ◽  
Ingrid Membrillo ◽  
Victor M. Ugalde-Saldívar ◽  
Laura Gasque
Keyword(s):  
Oxidase Activity ◽  
Copper Complexes ◽  
Theoretical Study ◽  
Imidazole Derivative ◽  
Catechol Oxidase ◽  
Dinuclear Copper

Comment on “Pressure-induced structural and valence transition in AgO” by C. Hou, J. Botana, X. Zhang, X. Wang and M. Miao, Phys. Chem. Chem. Phys., 2016, 18, 15322

2016 ◽  
Vol 18 (46) ◽  
pp. 31973-31974 ◽  
Author(s):  
Mariana Derzsi ◽  
Wojciech Grochala
Keyword(s):  
Electronic Structure ◽  
Recent Article ◽  
Theoretical Study ◽  
Mixed Valence ◽  
Chem Phys ◽  
External Pressure ◽  
Valence Transition ◽  
Mixed Valence Compound ◽  
Phys Chem Chem Phys

The recent article by Hou et al. has focused on a theoretical study of mixed valence compound AgO in order to elucidate the nature of the electronic structure of this system as a function of external pressure.

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

Theoretical Study on Novel Mixed Valence, P-H Functional P-Ligands, and Their Tautomerization

2014 ◽  
Vol 25 (6) ◽  
pp. 651-657 ◽  
Author(s):  
Arturo Espinosa ◽  
Liliya Abdrakhmanova ◽  
Rainer Streubel
Keyword(s):  
Theoretical Study ◽  
Mixed Valence ◽  
P Ligands

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.

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