Synthesis, Structure, and Properties of an Fe(II) Carbonyl [(PaPy3)Fe(CO)](ClO4):  Insight into the Reactivity of Fe(II)−CO and Fe(II)−NO Moieties in Non-Heme Iron Chelates of N-Donor Ligands

2006 ◽  
Vol 45 (9) ◽  
pp. 3774-3781 ◽  
Author(s):  
Raman K. Afshar ◽  
Apurba K. Patra ◽  
Eckhard Bill ◽  
Marilyn M. Olmstead ◽  
Pradip K. Mascharak
Keyword(s):  
Heme Iron ◽  
Donor Ligands ◽  
Structure And Properties ◽  
Iron Chelates ◽  
Non Heme Iron ◽  
Insight Into

Oxidative Degradation of Toxic Organic Pollutants by Water Soluble Nonheme Iron(IV)-Oxo Complexes of Polydentate Nitrogen Donor Ligands

2021 ◽  
Author(s):  
Sandip Munshi ◽  
Rahul Dev Jana ◽  
Tapan Kanti Paine
Keyword(s):  
Organic Pollutants ◽  
Oxidative Degradation ◽  
Heme Iron ◽  
Water Soluble ◽  
Donor Ligands ◽  
Nitrogen Donor Ligands ◽  
Polydentate Ligands ◽  
Oxo Complexes ◽  
Non Heme Iron ◽  
Nitrogen Donor

The ability of four mononuclear non-heme iron(IV)-oxo complexes supported by nitrogen donor polydentate ligands in degrading organic pollutants has been investigated. The water soluble iron(II) complexes upon treatment with ceric...

Mechanistic insight into halide oxidation by non-heme iron complexes. Haloperoxidase versus halogenase activity

2013 ◽  
Vol 49 (93) ◽  
pp. 10926 ◽  
Author(s):  
Anil Kumar Vardhaman ◽  
Prasenjit Barman ◽  
Suresh Kumar ◽  
Chivukula V. Sastri ◽  
Devesh Kumar ◽  
...  
Keyword(s):  
Iron Complexes ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Mechanistic Insight ◽  
Insight Into

scholarly journals Biochemical and crystallographic investigations into isonitrile formation by a non-heme iron-dependent oxidase/decarboxylase

2020 ◽  
pp. jbc.RA120.015932
Author(s):  
Rohan Jonnalagadda ◽  
Antonio Del Rio Flores ◽  
Welong Cai ◽  
Rimsha Mehmood ◽  
Maanasa Narayanamoorthy ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
Condensation Reaction ◽  
Enzymatic Reaction ◽  
Binding Pocket ◽  
Marine Sponges ◽  
Heme Iron ◽  
Site Directed Mutagenesis ◽  
Butanoic Acid ◽  
Non Heme Iron ◽  
Insight Into

The isonitrile moiety is found in marine sponges and some microbes, where it plays a role in processes such as virulence and metal acquisition. Until recently only one route was known for isonitrile biosynthesis, a condensation reaction that brings together a nitrogen atom of l-Trp/l-Tyr with a carbon atom from ribulose-5-phosphate. With the discovery of ScoE, a mononuclear Fe(II) α-ketoglutarate-dependent dioxygenase from Streptomyces coeruleorubidus, a second route was identified. ScoE forms isonitrile from a glycine adduct, with both the nitrogen and carbon atoms coming from the same glycyl moiety.  This reaction is part of the nonribosomal biosynthetic pathway of isonitrile lipopeptides. Here, we present structural, biochemical and computational investigations of the mechanism of isonitrile formation by ScoE, an unprecedented reaction in the mononuclear Fe(II) α-ketoglutarate-dependent dioxygenase superfamily. The stoichiometry of this enzymatic reaction is measured and multiple high-resolution (1.45-1.96 Å resolution) crystal structures of Fe(II)-bound ScoE are presented, providing insight into the binding of substrate, (R)-3-((carboxylmethyl)amino)butanoic acid (CABA), co-substrate α-ketoglutarate, and an Fe(IV)=O mimic oxovanadium. Comparison to a previously published crystal structure of ScoE suggests that ScoE has an ‘inducible’ α-ketoglutarate binding site, in which two residues arginine-157 and histidine-299 move by approximately 10 Å from the surface of the protein into the active site to create a transient α-ketoglutarate binding pocket.  Together, data from structural analyses, site-directed mutagenesis and computation, provide insight into the mode of α-ketoglutarate binding, the mechanism of isonitrile formation, and how the structure of ScoE has been adapted to perform this unusual chemical reaction.

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

Studies of iron(ii) and iron(iii) complexes with fac-N2O, cis-N2O2 and N2O3 donor ligands: models for the 2-His 1-carboxylate motif of non-heme iron monooxygenases

2012 ◽  
Vol 41 (18) ◽  
pp. 5662 ◽  
Author(s):  
Patrick J. Cappillino ◽  
John R. Miecznikowski ◽  
Laurie A. Tyler ◽  
Paul C. Tarves ◽  
Joshua S. McNally ◽  
...  
Keyword(s):  
Heme Iron ◽  
Donor Ligands ◽  
Non Heme Iron

scholarly journals Bioinspired Non-Heme Iron Complexes: The Evolution of Facial N, N, O Ligand Design

2020 ◽  
Vol 74 (6) ◽  
pp. 450-466
Author(s):  
Emily C. Monkcom ◽  
Pradip Ghosh ◽  
Emma Folkertsma ◽  
Hidde A. Negenman ◽  
Martin Lutz ◽  
...  
Keyword(s):  
Molecular Oxygen ◽  
Homogeneous Catalysis ◽  
Active Site ◽  
Ligand Design ◽  
Heme Iron ◽  
Donor Ligands ◽  
Non Heme Iron ◽  
Oxidative Transformations ◽  
Iron Based ◽  
Iron Based Catalysts

Iron-containing metalloenzymes that contain the 2-His-1-Carboxylate facial triad at their active site are well known for their ability to activate molecular oxygen and catalyse a broad range of oxidative transformations. Many of these reactions are synthetically challenging, and developing small molecular iron-based catalysts that can achieve similar reactivity and selectivity remains a long-standing goal in homogeneous catalysis. This review focuses on the development of bioinspired facial N,N,O ligands that model the 2-His-1-Carboxylate facial triad to a greater degree of structural accuracy than many of the polydentate N-donor ligands commonly used in this field. By developing robust, well-defined N,N,O facial ligands, an increased understanding could be gained of the factors governing enzymatic reactivity and selectivity.

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