Oxygenative cleavage of catechols including protocatechuic acid with molecular oxygen in water catalysed by water-soluble non-heme iron(iii) complexes in relevance to catechol dioxygenases

2002 ◽  
pp. 412-413 ◽  
Author(s):  
Takuzo Funabiki ◽  
Daisuke Sugio ◽  
Nobuhiko Inui ◽  
Matsutaka Maeda ◽  
Yutaka Hitomi
Keyword(s):  
Molecular Oxygen ◽  
Protocatechuic Acid ◽  
Heme Iron ◽  
Water Soluble ◽  
Non Heme Iron ◽  
Catechol Dioxygenases

Oxidative Degradation of Toxic Organic Pollutants by Water Soluble Nonheme Iron(IV)-Oxo Complexes of Polydentate Nitrogen Donor Ligands

2021 ◽  
Author(s):  
Sandip Munshi ◽  
Rahul Dev Jana ◽  
Tapan Kanti Paine
Keyword(s):  
Organic Pollutants ◽  
Oxidative Degradation ◽  
Heme Iron ◽  
Water Soluble ◽  
Donor Ligands ◽  
Nitrogen Donor Ligands ◽  
Polydentate Ligands ◽  
Oxo Complexes ◽  
Non Heme Iron ◽  
Nitrogen Donor

The ability of four mononuclear non-heme iron(IV)-oxo complexes supported by nitrogen donor polydentate ligands in degrading organic pollutants has been investigated. The water soluble iron(II) complexes upon treatment with ceric...

Mononuclear non-heme iron(III) complexes as functional models for catechol dioxygenases

2007 ◽  
Vol 10 (4-5) ◽  
pp. 366-379 ◽  
Author(s):  
Mallayan Palaniandavar ◽  
Ramasamy Mayilmurugan
Keyword(s):  
Heme Iron ◽  
Non Heme Iron ◽  
Functional Models ◽  
Catechol Dioxygenases

scholarly journals Bioinspired Non-Heme Iron Complexes: The Evolution of Facial N, N, O Ligand Design

2020 ◽  
Vol 74 (6) ◽  
pp. 450-466
Author(s):  
Emily C. Monkcom ◽  
Pradip Ghosh ◽  
Emma Folkertsma ◽  
Hidde A. Negenman ◽  
Martin Lutz ◽  
...  
Keyword(s):  
Molecular Oxygen ◽  
Homogeneous Catalysis ◽  
Active Site ◽  
Ligand Design ◽  
Heme Iron ◽  
Donor Ligands ◽  
Non Heme Iron ◽  
Oxidative Transformations ◽  
Iron Based ◽  
Iron Based Catalysts

Iron-containing metalloenzymes that contain the 2-His-1-Carboxylate facial triad at their active site are well known for their ability to activate molecular oxygen and catalyse a broad range of oxidative transformations. Many of these reactions are synthetically challenging, and developing small molecular iron-based catalysts that can achieve similar reactivity and selectivity remains a long-standing goal in homogeneous catalysis. This review focuses on the development of bioinspired facial N,N,O ligands that model the 2-His-1-Carboxylate facial triad to a greater degree of structural accuracy than many of the polydentate N-donor ligands commonly used in this field. By developing robust, well-defined N,N,O facial ligands, an increased understanding could be gained of the factors governing enzymatic reactivity and selectivity.

Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD

2019 ◽  
Author(s):  
Christopher John ◽  
Greg M. Swain ◽  
Robert P. Hausinger ◽  
Denis A. Proshlyakov
Keyword(s):  
Active Site ◽  
Structural Model ◽  
Heme Iron ◽  
Chemical Transformations ◽  
Experimental Conditions ◽  
Strongly Coupled ◽  
Non Heme Iron ◽  
Reversible Redox ◽  
Wide Range ◽  
Complex Structural

2-Oxoglutarate (2OG)-dependent dioxygenases catalyze C-H activation while performing a wide range of chemical transformations. In contrast to their heme analogues, non-heme iron centers afford greater structural flexibility with important implications for their diverse catalytic mechanisms. We characterize an <i>in situ</i> structural model of the putative transient ferric intermediate of 2OG:taurine dioxygenase (TauD) by using a combination of spectroelectrochemical and semi-empirical computational methods, demonstrating that the Fe (III/II) transition involves a substantial, fully reversible, redox-linked conformational change at the active site. This rearrangement alters the apparent redox potential of the active site between -127 mV for reduction of the ferric state and 171 mV for oxidation of the ferrous state of the 2OG-Fe-TauD complex. Structural perturbations exhibit limited sensitivity to mediator concentrations and potential pulse duration. Similar changes were observed in the Fe-TauD and taurine-2OG-Fe-TauD complexes, thus attributing the reorganization to the protein moiety rather than the cosubstrates. Redox difference infrared spectra indicate a reorganization of the protein backbone in addition to the involvement of carboxylate and histidine ligands. Quantitative modeling of the transient redox response using two alternative reaction schemes across a variety of experimental conditions strongly supports the proposal for intrinsic protein reorganization as the origin of the experimental observations.

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