scholarly journals The role of spin states in the catalytic mechanism of the intra- and extradiol cleavage of catechols by O2

2017 ◽  
Vol 15 (37) ◽  
pp. 7860-7868 ◽  
Author(s):  
S. Stepanović ◽  
D. Angelone ◽  
M. Gruden ◽  
M. Swart
Keyword(s):  
Spin State ◽  
Catalytic Mechanism ◽  
Spin States ◽  
Density Functionals

Intradiol vs. extradiol selectivity of Fe(iii)-complexes explained by spin-state consistent density functionals.

Study of the catalytic mechanism of a non-heme Fe catalyst: The role of the spin state of the iron

2021 ◽  
Vol 764 ◽  
pp. 138282
Author(s):  
Aikaterini Gemenetzi ◽  
Panagiota Stathi ◽  
Yiannis Deligiannakis ◽  
Maria Louloudi
Keyword(s):  
Spin State ◽  
Catalytic Mechanism ◽  
Fe Catalyst

scholarly journals The role of symmetry breaking in the structural trapping of light-induced excited spin states

2017 ◽  
Vol 53 (99) ◽  
pp. 13268-13271 ◽  
Author(s):  
Rafal Kulmaczewski ◽  
Elzbieta Trzop ◽  
Laurence J. Kershaw Cook ◽  
Eric Collet ◽  
Guillaume Chastanet ◽  
...  
Keyword(s):  
Symmetry Breaking ◽  
Spin State ◽  
Spin States ◽  
Crystallographic Symmetry ◽  
Red Line

Six isostructural compounds show differing agreement with the correlation T(LIESST) = T0 − 0.3T1/2 (red line; LIESST = Light-Induced Excited Spin-State Trapping). This reflects crystallographic symmetry breaking under LIESST conditions, exhibited by one of the compounds but not by two others.

scholarly journals Density Functional Approximations for Consistent Spin and Oxidation States of Oxoiron Complexes

2019 ◽  
Author(s):  
Filip Vlahovic ◽  
Maja Gruden ◽  
Stepan Stepanović ◽  
Marcel Swart
Keyword(s):  
Oxidation State ◽  
Spin State ◽  
Density Functional ◽  
Computational Study ◽  
Relativistic Effects ◽  
Oxidation States ◽  
Spin States ◽  
Density Functionals ◽  
Computational Tool ◽  
Excellent Performance

We report here a computational study on a series of Fe<sup>II</sup>, Fe<sup>III</sup>and Fe<sup>IV</sup>hydroxo/oxo-iron complexes with a broad palette of ligands. We are interested in assessing the robustness of widely used density functionals for their prediction and description of structures and spin states for the examined oxoiron complexes. We have used a variety of density functional approximations (S12g, LDA, BP86<a>-D<sub>3</sub></a>, OPBE, SSB-D, B3LYP-D<sub>3</sub>, S12h and MVS), in all cases including solvation and relativistic effects explicitly. One of the main observations of this detailed study is the excellent performance of S12g for both accurate structures and spin state splittings. Moreover, our results show that in general all density functionals can be used as a reliable computational tool for reproducing and predicting geometries, determining the oxidation state of iron, and most are able as well to providing good descriptions of spin state energetics.

Density Functional Approximations for Consistent Spin and Oxidation States of Oxoiron Complexes

2019 ◽  
Author(s):  
Filip Vlahovic ◽  
Maja Gruden ◽  
Stepan Stepanović ◽  
Marcel Swart
Keyword(s):  
Oxidation State ◽  
Spin State ◽  
Density Functional ◽  
Computational Study ◽  
Relativistic Effects ◽  
Oxidation States ◽  
Spin States ◽  
Density Functionals ◽  
Computational Tool ◽  
Excellent Performance

We report here a computational study on a series of Fe<sup>II</sup>, Fe<sup>III</sup>and Fe<sup>IV</sup>hydroxo/oxo-iron complexes with a broad palette of ligands. We are interested in assessing the robustness of widely used density functionals for their prediction and description of structures and spin states for the examined oxoiron complexes. We have used a variety of density functional approximations (S12g, LDA, BP86<a>-D<sub>3</sub></a>, OPBE, SSB-D, B3LYP-D<sub>3</sub>, S12h and MVS), in all cases including solvation and relativistic effects explicitly. One of the main observations of this detailed study is the excellent performance of S12g for both accurate structures and spin state splittings. Moreover, our results show that in general all density functionals can be used as a reliable computational tool for reproducing and predicting geometries, determining the oxidation state of iron, and most are able as well to providing good descriptions of spin state energetics.

Role of Lys-226 in the Catalytic Mechanism ofBacillus StearothermophilusSerine HydroxymethyltransferaseCrystal Structure and Kinetic Studies†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (18) ◽  
pp. 6929-6937 ◽  
Author(s):  
Siddegowda Bhavani ◽  
V. Trivedi ◽  
V. R. Jala ◽  
H. S. Subramanya ◽  
Purnima Kaul ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Kinetic Studies

Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism

2001 ◽  
Vol 359 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Valeria MENCHISE ◽  
Catherine CORBIER ◽  
Claude DIDIERJEAN ◽  
Michele SAVIANO ◽  
Ettore BENEDETTI ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Proton Transfer ◽  
Chlamydomonas Reinhardtii ◽  
Catalytic Mechanism ◽  
Structural Data ◽  
Careful Analysis ◽  
Wild Type ◽  
Thioredoxin H ◽  
Dynamics Simulations

Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.

Structure−Function Relationships in Human Glutathione-Dependent Formaldehyde Dehydrogenase. Role of Glu-67 and Arg-368 in the Catalytic Mechanism†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (15) ◽  
pp. 4819-4830 ◽  
Author(s):  
Paresh C. Sanghani ◽  
Wilhelmina I. Davis ◽  
LanMin Zhai ◽  
Howard Robinson
Keyword(s):  
Structure Function ◽  
Catalytic Mechanism ◽  
Formaldehyde Dehydrogenase
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