ChemInform Abstract: Selective Conversion of Hydrocarbons with H2O2Using Biomimetic Non-Heme Iron and Manganese Oxidation Catalysts

ChemInform ◽  
2009 ◽  
Vol 40 (9) ◽  
Author(s):  
Stefania Tanase ◽  
Elisabeth Bouwman
Keyword(s):  
Heme Iron ◽  
Oxidation Catalysts ◽  
Manganese Oxidation ◽  
Selective Conversion ◽  
Non Heme Iron ◽  
Iron And Manganese

Towards robust alkane oxidation catalysts: electronic variations in non-heme iron(ii) complexes and their effect in catalytic alkane oxidation

2009 ◽  
pp. 5319 ◽  
Author(s):  
Jason England ◽  
Reema Gondhia ◽  
Laura Bigorra-Lopez ◽  
Allan R. Petersen ◽  
Andrew J. P. White ◽  
...  
Keyword(s):  
Heme Iron ◽  
Alkane Oxidation ◽  
Oxidation Catalysts ◽  
Non Heme Iron

scholarly journals Deuterated N2Py2 Ligands: Building More Robust Non-Heme Iron Oxidation Catalysts

ACS Catalysis ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 3564-3575 ◽  
Author(s):  
Jianming Chen ◽  
Robertus J. M. Klein Gebbink
Keyword(s):  
Iron Oxidation ◽  
Heme Iron ◽  
Oxidation Catalysts ◽  
Non Heme Iron

Lignin-Derived Non-Heme Iron and Manganese Complexes: Catalysts for the On-Demand Production of Chlorine Dioxide in Water under Mild Conditions

2021 ◽  
Vol 60 (5) ◽  
pp. 2905-2913
Author(s):  
Tayyebeh B. Champ ◽  
Jun H. Jang ◽  
Justin L. Lee ◽  
Guang Wu ◽  
Michael A. Reynolds ◽  
...  
Keyword(s):  
Chlorine Dioxide ◽  
Heme Iron ◽  
Manganese Complexes ◽  
Mild Conditions ◽  
On Demand ◽  
Non Heme Iron ◽  
Iron And Manganese

Mechanism of water oxidation by non-heme iron catalysts when driven with sodium periodate

2014 ◽  
Vol 43 (33) ◽  
pp. 12501-12513 ◽  
Author(s):  
Alexander R. Parent ◽  
Takashi Nakazono ◽  
Shu Lin ◽  
Satoshi Utsunomiya ◽  
Ken Sakai
Keyword(s):  
Water Oxidation ◽  
Sodium Periodate ◽  
Iron Complexes ◽  
Heme Iron ◽  
Iron Catalysts ◽  
Dinuclear Complexes ◽  
Oxidation Catalysts ◽  
Monomeric Species ◽  
Non Heme Iron

Non-heme iron complexes were determined to serve as homogeneous water oxidation catalysts when driven with sodium periodate. Both mononuclear and dinuclear complexes were found to be active for water oxidation, with the monomeric species exhibiting higher rates.

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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