scholarly journals A Combined NRVS and DFT Study of FeIVO Model Complexes: A Diagnostic Method for the Elucidation of Non-Heme Iron Enzyme Intermediates

2008 ◽  
Vol 47 (47) ◽  
pp. 9071-9074 ◽  
Author(s):  
Caleb B. Bell ◽  
Shaun D. Wong ◽  
Yuming Xiao ◽  
Eric J. Klinker ◽  
Adam L. Tenderholt ◽  
...  
Keyword(s):  
Diagnostic Method ◽  
Heme Iron ◽  
Dft Study ◽  
Model Complexes ◽  
Non Heme Iron ◽  
Enzyme Intermediates

A Combined NRVS and DFT Study of FeIVO Model Complexes: A Diagnostic Method for the Elucidation of Non-Heme Iron Enzyme Intermediates

2008 ◽  
Vol 120 (47) ◽  
pp. 9211-9214 ◽  
Author(s):  
Caleb B. Bell ◽  
Shaun D. Wong ◽  
Yuming Xiao ◽  
Eric J. Klinker ◽  
Adam L. Tenderholt ◽  
...  
Keyword(s):  
Diagnostic Method ◽  
Heme Iron ◽  
Dft Study ◽  
Model Complexes ◽  
Non Heme Iron ◽  
Enzyme Intermediates

scholarly journals Deciphering the mechanism of O2 reduction with electronically tunable non-heme iron enzyme model complexes

2018 ◽  
Vol 9 (26) ◽  
pp. 5773-5780 ◽  
Author(s):  
Roshaan Surendhran ◽  
Alexander A. D'Arpino ◽  
Bao Y. Sciscent ◽  
Anthony F. Cannella ◽  
Alan E. Friedman ◽  
...  
Keyword(s):  
Homologous Series ◽  
Heme Iron ◽  
Model Complexes ◽  
Non Heme Iron ◽  
O2 Reduction ◽  
Enzyme Model ◽  
Fe Complexes ◽  
Electronically Tunable

A homologous series of electronically tuned ligands were prepared and some of their corresponding Fe complexes were prepared and a Hammett plot of the rates of O2 reduction allowed us to infer important details of the mechanism.

Hydrogen Peroxide Decomposition by a Non-Heme Iron(III) Catalase Mimic: A DFT Study

2007 ◽  
Vol 13 (15) ◽  
pp. 4230-4245 ◽  
Author(s):  
Willi Sicking ◽  
Hans-Gert Korth ◽  
Georg Jansen ◽  
Herbert de Groot ◽  
Reiner Sustmann
Keyword(s):  
Hydrogen Peroxide ◽  
Heme Iron ◽  
Dft Study ◽  
Hydrogen Peroxide Decomposition ◽  
Non Heme Iron ◽  
Peroxide Decomposition

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.

Sign in / Sign up

Export Citation Format

Share Document