Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance

Biochemistry ◽  
1991 ◽  
Vol 30 (29) ◽  
pp. 7349-7358 ◽  
Author(s):  
Joan B. Broderick ◽  
Thomas V. O'Halloran
Keyword(s):  
Heme Iron ◽  
Purification And Characterization ◽  
Non Heme Iron ◽  
Substrate Tolerance

Activation of dioxygen by a mononuclear non-heme iron complex: characterization of a FeIII(OOH) intermediate

2010 ◽  
Vol 39 (6) ◽  
pp. 1630-1634 ◽  
Author(s):  
Marlène Martinho ◽  
Guillaume Blain ◽  
Frédéric Banse
Keyword(s):  
Iron Complex ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Complex Characterization

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.

scholarly journals Rapid purification of rabbit reticulocyte lipoxygenase for electron paramagnetic spectroscopy characterization of the non-heme iron

Lipids ◽  
1993 ◽  
Vol 28 (3) ◽  
pp. 241-244 ◽  
Author(s):  
Richard T. Carroll ◽  
Jessica Muller ◽  
Jennifer Grimm ◽  
William R. Dunham ◽  
Richard H. Sands ◽  
...  
Keyword(s):  
Heme Iron ◽  
Non Heme Iron ◽  
Rapid Purification ◽  
Electron Paramagnetic Spectroscopy ◽  
Electron Paramagnetic

Characterization of Mononuclear Non-heme Iron(III)-Superoxo Complex with a Five-Azole Ligand Set

2015 ◽  
Vol 54 (25) ◽  
pp. 7336-7339 ◽  
Author(s):  
Frédéric Oddon ◽  
Yosuke Chiba ◽  
Jun Nakazawa ◽  
Takehiro Ohta ◽  
Takashi Ogura ◽  
...  
Keyword(s):  
Heme Iron ◽  
Non Heme Iron

Synthesis and characterization of a family of binuclear non-heme iron monooxygenase model compounds: Evidence for a “phenolate/amide carbonyl (PAC) shift” upon oxidation

2009 ◽  
Vol 362 (7) ◽  
pp. 2136-2150 ◽  
Author(s):  
Patrick J. Cappillino ◽  
Paul C. Tarves ◽  
Gerard T. Rowe ◽  
Andrew J. Lewis ◽  
Mark Harvey ◽  
...  
Keyword(s):  
Heme Iron ◽  
Synthesis And Characterization ◽  
Model Compounds ◽  
Non Heme Iron ◽  
Amide Carbonyl
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