2020
DOI: 10.1016/j.ica.2020.119480
|View full text |Cite
|
Sign up to set email alerts
|

Catalytic promiscuity of a copper(II)-Mannich base complex having unprecedented radical pathway in catecholase activity

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

1
9
0

Year Published

2020
2020
2024
2024

Publication Types

Select...
9

Relationship

1
8

Authors

Journals

citations
Cited by 15 publications
(10 citation statements)
references
References 68 publications
1
9
0
Order By: Relevance
“…The reason for the better catalytic properties of the Fe(III) complexes over the Cu(II) complexes may be attributed to sthe higher reduction potential of their metal center which is a vital process in the catalytic process. Comparable or higher values of kcat have also been observed in some previous studies with the nature of the solvent playing a great role [44,45]. It is believed that a less coordinating solvent than DMF may result in higher turnover rates because of a more favourable formation of the metal-substrate adduct.…”
Section: Evaluation Of Catecholase Activitiessupporting
confidence: 57%
“…The reason for the better catalytic properties of the Fe(III) complexes over the Cu(II) complexes may be attributed to sthe higher reduction potential of their metal center which is a vital process in the catalytic process. Comparable or higher values of kcat have also been observed in some previous studies with the nature of the solvent playing a great role [44,45]. It is believed that a less coordinating solvent than DMF may result in higher turnover rates because of a more favourable formation of the metal-substrate adduct.…”
Section: Evaluation Of Catecholase Activitiessupporting
confidence: 57%
“…Phosphatase is an assemblage of hydrolytic enzymes that catalyze the dephosphorylation reaction, that is, hydrolysis of phosphate monoesteric, diesteric, and triesteric P–O bonds This is one of the essential biological reactions, as this is involved in cellular signaling, synthesis of proteins, replication of genetic material to energy, and so forth. , The uncatalyzed hydrolysis is extremely slow and the cleavage of P–O bonds is accelerated in the presence of bivalent metal ions. Over the last few decades, many groups including our group have been involved in designing the bio-mimicking models to establish plausible mechanistic pathways of phosphatase activity. Generally, dinuclear complexes are more efficient than their mononuclear counterparts because two metal centers may act mutually in substrate binding to catalyst, activation of the nucleophile, and cleavage of the bond. The availability of a nucleophile (water or hydroxo) in the close vicinity of the metal center(s) is the predominant factor of phosphatase activity and attack of nucleophile on the phosphorus center is the rate-determining step of hydrolysis . The other factors that dictate the rate of hydrolysis are reaction conditions, Lewis acidity of metal centers, stereochemistry, presence of oxo-anions, the coordination domain of metal ions, and the presence of electronegative atoms in the ligand backbone. In recent times, designing of bio-mimicking models with additional biological applications always draws special attention of the bio-inorganic chemists . The incorporation of metals to the ligand system enhanced the biological activity of the overall entity.…”
Section: Introductionmentioning
confidence: 99%
“…Table 2 Comparison table of the phosphatase activity of some copper(II) and nickel(II) complexes described in the literature [40][41][42][43] Catalyst Solvent K cat (h À1 ) Ref.…”
Section: One Of the Important Examples Inmentioning
confidence: 99%