scholarly journals Spectroscopy of Non-Heme Iron Thiolate Complexes:  Insight into the Electronic Structure of the Low-Spin Active Site of Nitrile Hydratase

2005 ◽  
Vol 44 (6) ◽  
pp. 1826-1836 ◽  
Author(s):  
Pierre Kennepohl ◽  
Frank Neese ◽  
Dirk Schweitzer ◽  
Henry L. Jackson ◽  
Julie A. Kovacs ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Active Site ◽  
Nitrile Hydratase ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Thiolate Complexes ◽  
Iron Thiolate ◽  
Insight Into

scholarly journals Sulfur K-Edge XAS and DFT Calculations on Nitrile Hydratase:  Geometric and Electronic Structure of the Non-heme Iron Active Site

2006 ◽  
Vol 128 (2) ◽  
pp. 533-541 ◽  
Author(s):  
Abhishek Dey ◽  
Marina Chow ◽  
Kayoko Taniguchi ◽  
Priscilla Lugo-Mas ◽  
Steven Davin ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Dft Calculations ◽  
Active Site ◽  
Nitrile Hydratase ◽  
Heme Iron ◽  
Non Heme Iron

scholarly journals Sulfur oxygenation in biomimetic non-heme iron–thiolate complexes

2012 ◽  
Vol 41 (36) ◽  
pp. 10883 ◽  
Author(s):  
Alison C. McQuilken ◽  
David P. Goldberg
Keyword(s):  
Heme Iron ◽  
Non Heme Iron ◽  
Thiolate Complexes ◽  
Iron Thiolate

Spectroscopic Definition of the Geometric and Electronic Structure of the Non-Heme Iron Active Site in Iron(II) Bleomycin: Correlation with Oxygen Reactivity

1995 ◽  
Vol 117 (16) ◽  
pp. 4545-4561 ◽  
Author(s):  
Kelly E. Loeb ◽  
Jeffrey M. Zaleski ◽  
Tami E. Westre ◽  
Richard J. Guajardo ◽  
Pradip K. Mascharak ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Active Site ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Definition Of ◽  
Oxygen Reactivity

ChemInform Abstract: Sulfur Oxygenation in Biomimetic Non-Heme Iron-Thiolate Complexes

ChemInform ◽  
2012 ◽  
Vol 43 (50) ◽  
pp. no-no
Author(s):  
Alison C. McQuilken ◽  
David P. Goldberg
Keyword(s):  
Heme Iron ◽  
Non Heme Iron ◽  
Thiolate Complexes ◽  
Iron Thiolate

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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