Reactivity of the Binuclear Non-Heme Iron Active Site of Δ9 Desaturase Studied by Large-Scale Multireference Ab Initio Calculations

2014 ◽  
Vol 136 (45) ◽  
pp. 15977-15991 ◽  
Author(s):  
Jakub Chalupský ◽  
Tibor András Rokob ◽  
Yuki Kurashige ◽  
Takeshi Yanai ◽  
Edward I. Solomon ◽  
...  
Keyword(s):  
Ab Initio Calculations ◽  
Ab Initio ◽  
Active Site ◽  
Large Scale ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Δ9 Desaturase

Ab Initio Calculations for Spin-Gaps of Non-Heme Iron Complexes

2019 ◽  
Vol 15 (8) ◽  
pp. 4297-4304 ◽  
Author(s):  
Quan Manh Phung ◽  
Carlos Martín-Fernández ◽  
Jeremy N. Harvey ◽  
Milica Feldt
Keyword(s):  
Ab Initio Calculations ◽  
Ab Initio ◽  
Iron Complexes ◽  
Heme Iron ◽  
Non Heme Iron

Energetics of non-heme iron reactivity: can ab initio calculations provide the right answer?

2020 ◽  
Vol 22 (41) ◽  
pp. 23908-23919
Author(s):  
Milica Feldt ◽  
Carlos Martín-Fernández ◽  
Jeremy N. Harvey
Keyword(s):  
Hydrogen Atom ◽  
Ab Initio Calculations ◽  
Ab Initio ◽  
Computational Methods ◽  
Hydrogen Atom Transfer ◽  
Heme Iron ◽  
Reaction Pathways ◽  
Non Heme Iron ◽  
Epoxidation Reaction ◽  
The Right

We use a variety of computational methods to characterize and compare the hydrogen atom transfer (HAT) and epoxidation reaction pathways for oxidation of cyclohexene by an iron(iv)-oxo complex.

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.

Revisiting Mulliken’s Concepts about Rydberg States and Rydberg−Valence Interactions from Large-Scale Ab Initio Calculations on the Acetylene Molecule†

2009 ◽  
Vol 113 (47) ◽  
pp. 13210-13220 ◽  
Author(s):  
Fabrice Laruelle ◽  
Séverine Boyé-Péronne ◽  
Dolores Gauyacq ◽  
Jacques Liévin
Keyword(s):  
Ab Initio Calculations ◽  
Ab Initio ◽  
Large Scale ◽  
Rydberg States ◽  
Acetylene Molecule

scholarly journals Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD

2019 ◽  
Vol 123 (37) ◽  
pp. 7785-7793 ◽  
Author(s):  
Christopher W. John ◽  
Greg M. Swain ◽  
Robert P. Hausinger ◽  
Denis A. Proshlyakov
Keyword(s):  
Active Site ◽  
Heme Iron ◽  
Conformational Switching ◽  
Strongly Coupled ◽  
Non Heme Iron

Evidence for the involvement of non-heme iron in the active site of hydrogenase from Desulfovibrio vulgaris

1971 ◽  
Vol 234 (3) ◽  
pp. 525-530 ◽  
Author(s):  
J. Legall ◽  
D.V. Dervartanian ◽  
E. Spilker ◽  
Jin-Po Lee ◽  
H.D. Peck
Keyword(s):  
Active Site ◽  
Heme Iron ◽  
Desulfovibrio Vulgaris ◽  
Non Heme Iron

scholarly journals Structural characterization of a non-heme iron active site in zeolites that hydroxylates methane

2018 ◽  
Vol 115 (18) ◽  
pp. 4565-4570 ◽  
Author(s):  
Benjamin E. R. Snyder ◽  
Lars H. Böttger ◽  
Max L. Bols ◽  
James J. Yan ◽  
Hannah M. Rhoda ◽  
...  
Keyword(s):  
Active Site ◽  
Density Functional ◽  
Density Functional Theory Calculations ◽  
Heme Iron ◽  
Zeolite Lattice ◽  
Non Heme Iron ◽  
Bonding Interaction ◽  
Lattice Density ◽  
X Ray Absorption

Iron-containing zeolites exhibit unprecedented reactivity in the low-temperature hydroxylation of methane to form methanol. Reactivity occurs at a mononuclear ferrous active site, α-Fe(II), that is activated by N2O to form the reactive intermediate α-O. This has been defined as an Fe(IV)=O species. Using nuclear resonance vibrational spectroscopy coupled to X-ray absorption spectroscopy, we probe the bonding interaction between the iron center, its zeolite lattice-derived ligands, and the reactive oxygen. α-O is found to contain an unusually strong Fe(IV)=O bond resulting from a constrained coordination geometry enforced by the zeolite lattice. Density functional theory calculations clarify how the experimentally determined geometric structure of the active site leads to an electronic structure that is highly activated to perform H-atom abstraction.

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