Two-State Reactivity in Alkane Hydroxylation by Non-Heme Iron−Oxo Complexes

2006 ◽  
Vol 128 (26) ◽  
pp. 8590-8606 ◽  
Author(s):  
Hajime Hirao ◽  
Devesh Kumar ◽  
Lawrence Que ◽  
Sason Shaik
Keyword(s):  
Heme Iron ◽  
Oxo Complexes ◽  
Non Heme Iron ◽  
Alkane Hydroxylation

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...

A non-heme cationic Fe(iii)-complex intercalated in montmorillonite K-10: synthesis, characterization and catalytic alkane hydroxylation with H2O2 at room temperature

2014 ◽  
Vol 4 (9) ◽  
pp. 3180-3185 ◽  
Author(s):  
Anand Pariyar ◽  
Suranjana Bose ◽  
Achintesh Narayan Biswas ◽  
Sudip Barman ◽  
Pinaki Bandyopadhyay
Keyword(s):  
Room Temperature ◽  
Heme Iron ◽  
Environmentally Benign ◽  
Efficient Catalyst ◽  
Non Heme Iron ◽  
Alkane Hydroxylation ◽  
Selective Hydroxylation

An efficient catalyst for highly selective hydroxylation of alkanes with environmentally benign H2O2 at room temperature has been designed by the intercalation of a non-heme iron(iii) complex into smectite montmorillonite K-10.

scholarly journals Regio‐selective alkane hydroxylation by the isolated membrane‐bound non‐heme iron oxygenase, AlkB

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Wen‐I Luo ◽  
Chun‐Wei Chang ◽  
Ravirala Ramu ◽  
Yi‐Fang Tsai ◽  
Kok Yaoh Ng ◽  
...  
Keyword(s):  
Heme Iron ◽  
Non Heme Iron ◽  
Alkane Hydroxylation ◽  
Membrane Bound

scholarly journals Engineering the Oxidative Potency of Non-Heme Iron(IV) Oxo Complexes in Water for C–H Oxidation by a cis Donor and Variation of the Second Coordination Sphere

2021 ◽  
Vol 60 (3) ◽  
pp. 1975-1984
Author(s):  
Christina Wegeberg ◽  
Mathias L. Skavenborg ◽  
Andrea Liberato ◽  
James N. McPherson ◽  
Wesley R. Browne ◽  
...  
Keyword(s):  
Coordination Sphere ◽  
Heme Iron ◽  
Oxo Complexes ◽  
Non Heme Iron ◽  
Second Coordination Sphere

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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