An active-site model for nitrile hydratase: axially coordinate non-heme iron complexes in the low-spin ferric state

1988 ◽  
Vol 27 (22) ◽  
pp. 3877-3879 ◽  
Author(s):  
Hiromu Sakurai ◽  
Koichiro Tsuchiya ◽  
Kouto Migita
Keyword(s):  
Active Site ◽  
Nitrile Hydratase ◽  
Iron Complexes ◽  
Heme Iron ◽  
Site Model ◽  
Non Heme Iron ◽  
Active Site Model

scholarly journals A bioinspired oxoiron(iv) motif supported on a N2S2 macrocyclic ligand

2021 ◽  
Author(s):  
Jennifer Deutscher ◽  
Philipp Gerschel ◽  
Katrin Warm ◽  
Uwe Kuhlmann ◽  
Stefan Mebs ◽  
...  
Keyword(s):  
Active Site ◽  
Macrocyclic Ligand ◽  
Heme Iron ◽  
Site Model ◽  
Non Heme Iron ◽  
Active Site Model

A mononuclear oxoiron(iv) complex 1-trans bearing two equatorial sulfur ligations is synthesized and characterized as an active-site model of the elusive sulfur-ligated FeIVO intermediates in non-heme iron oxygenases.

Density functional study on geometry and electronic structure of nitrile hydratase active site model

2002 ◽  
Vol 90 (3) ◽  
pp. 1174-1187 ◽  
Author(s):  
W. Nowak ◽  
Y. Ohtsuka ◽  
J. Hasegawa ◽  
H. Nakatsuji
Keyword(s):  
Electronic Structure ◽  
Active Site ◽  
Density Functional ◽  
Nitrile Hydratase ◽  
Functional Study ◽  
Density Functional Study ◽  
Site Model ◽  
Active Site Model

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

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.

Structural and Spectroscopic Features of acis(Hydroxo)-FeIII-(Carboxylato) Configuration as an Active Site Model for Lipoxygenases

2002 ◽  
Vol 41 (21) ◽  
pp. 5513-5520 ◽  
Author(s):  
Seiji Ogo ◽  
Ryo Yamahara ◽  
Mark Roach ◽  
Tomoyoshi Suenobu ◽  
Michihiko Aki ◽  
...  
Keyword(s):  
Active Site ◽  
Site Model ◽  
Active Site Model
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