scholarly journals A Functional Model for the Cysteinate-Ligated Non-Heme Iron Enzyme Superoxide Reductase (SOR)

2006 ◽  
Vol 128 (45) ◽  
pp. 14448-14449 ◽  
Author(s):  
Terutaka Kitagawa ◽  
Abhishek Dey ◽  
Priscilla Lugo-Mas ◽  
Jason B. Benedict ◽  
Werner Kaminsky ◽  
...  
Keyword(s):  
Functional Model ◽  
Heme Iron ◽  
Superoxide Reductase ◽  
Non Heme Iron

Computational Study of the Non-Heme Iron Active Site in Superoxide Reductase and Its Reaction with Superoxide

2003 ◽  
Vol 42 (2) ◽  
pp. 446-456 ◽  
Author(s):  
Radu Silaghi-Dumitrescu ◽  
Ioan Silaghi-Dumitrescu ◽  
Eric D. Coulter ◽  
Donald M. Kurtz
Keyword(s):  
Active Site ◽  
Computational Study ◽  
Heme Iron ◽  
Superoxide Reductase ◽  
Non Heme Iron

scholarly journals Non-heme iron hydroperoxo species in superoxide reductase as a catalyst for oxidation reactions

2014 ◽  
Vol 50 (91) ◽  
pp. 14213-14216 ◽  
Author(s):  
S. Rat ◽  
S. Ménage ◽  
F. Thomas ◽  
V. Nivière
Keyword(s):  
High Spin ◽  
Ferric Iron ◽  
Heme Iron ◽  
Superoxide Reductase ◽  
Oxidation Reactions ◽  
Non Heme Iron

The non-heme high-spin ferric iron hydroperoxo species formed in superoxide reductase can act both as a nucleophile and as an electrophile to catalyze oxidation reactions.

scholarly journals Computational Study of the Non-Heme Iron Active Site in Superoxide Reductase and Its Reaction with Superoxide.

2003 ◽  
Vol 42 (5) ◽  
pp. 1786-1786
Author(s):  
Radu Silaghi-Dumitrescu ◽  
Ioan Silaghi-Dumitrescu ◽  
Eric D. Coulter ◽  
Donald M. Kurtz
Keyword(s):  
Active Site ◽  
Computational Study ◽  
Heme Iron ◽  
Superoxide Reductase ◽  
Non Heme Iron

Understanding the mechanism of superoxide reduction by the non-heme iron enzyme superoxide reductase (SOR) using a synthetic analogue approach

2003 ◽  
Vol 96 (1) ◽  
pp. 20
Author(s):  
Julie A. Kovacs ◽  
Sarah Fitch ◽  
Roslyn Theisen ◽  
Jason Shearer ◽  
Terry Kitagawa ◽  
...  
Keyword(s):  
Heme Iron ◽  
Superoxide Reductase ◽  
Synthetic Analogue ◽  
Non Heme Iron

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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