The ultrastrong and short intramolecular NHFe hydrogen bond in diferrocenyl hydrazone raises the barrier for intramolecular electron transfer in its mixed-valent cation and is only disrupted by double oxidation to .
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Electrostatically regulated active site assembly governs reactivity in non-heme iron halogenases.
bioRxiv
May 2023
Department of Chemistry, University of Minnesota, Twin Cities, Minneapolis, MN 55455, USA.
Non-heme iron halogenases (NHFe-Hals) catalyze the direct insertion of a chloride/bromide ion at an unactivated carbon position using a high-valent haloferryl intermediate. Despite more than a decade of structural and mechanistic characterization, how NHFe-Hals preferentially bind specific anions and substrates for C-H functionalization remains unknown. Herein, using lysine halogenating BesD and HalB enzymes as model systems, we demonstrate strong positive cooperativity between anion and substrate binding to the catalytic pocket.
View Article and Find Full Text PDFProton-Electron Transfer to the Active Site Is Essential for the Reaction Mechanism of Soluble Δ-Desaturase.
J Am Chem Soc
June 2020
J. Heyrovský Institute of Physical Chemistry, The Czech Academy of Sciences, Dolejškova 3, Prague 8 182 23, Czech Republic.
A full understanding of the catalytic action of non-heme iron (NHFe) and non-heme diiron (NHFe) enzymes is still beyond the grasp of contemporary computational and experimental techniques. Many of these enzymes exhibit fascinating chemo-, regio-, and stereoselectivity, in spite of employing highly reactive intermediates which are necessary for activations of most stable chemical bonds. Herein, we study in detail one intriguing representative of the NHFe family of enzymes: soluble Δ desaturase (ΔD), which desaturates rather than performing the thermodynamically favorable hydroxylation of substrate.
View Article and Find Full Text PDFDiferrocenyl tosyl hydrazone with an ultrastrong NHFe hydrogen bond as double click switch.
Chem Commun (Camb)
January 2015
Institute of Inorganic Chemistry and Analytical Chemistry, Johannes Gutenberg-University of Mainz, Duesbergweg 10-14, 55128 Mainz, Germany.
The ultrastrong and short intramolecular NHFe hydrogen bond in diferrocenyl hydrazone raises the barrier for intramolecular electron transfer in its mixed-valent cation and is only disrupted by double oxidation to .
View Article and Find Full Text PDFElucidation of the Fe(IV)=O intermediate in the catalytic cycle of the halogenase SyrB2.
Nature
July 2013
Department of Chemistry, Stanford University, Stanford, California 94305, USA.
Mononuclear non-haem iron (NHFe) enzymes catalyse a broad range of oxidative reactions, including halogenation, hydroxylation, ring closure, desaturation and aromatic ring cleavage reactions. They are involved in a number of biological processes, including phenylalanine metabolism, the production of neurotransmitters, the hypoxic response and the biosynthesis of secondary metabolites. The reactive intermediate in the catalytic cycles of these enzymes is a high-spin S = 2 Fe(IV)=O species, which has been trapped for a number of NHFe enzymes, including the halogenase SyrB2 (syringomycin biosynthesis enzyme 2).
View Article and Find Full Text PDFMetal-catalyzed anaerobic disproportionation of hydroxylamine. Role of diazene and nitroxyl intermediates in the formation of N2, N2O, NO+, and NH3.
J Am Chem Soc
October 2004
Departamento de Química, Facultad de Ciencias Exactas, Universidad Nacional de Mar del Plata, Funes y R. Peña, Mar del Plata B7602AYL, Argentina.
The catalytic disproportionation of NH(2)OH has been studied in anaerobic aqueous solution, pH 6-9.3, at 25.0 degrees C, with Na(3)[Fe(CN)(5)NH(3)].
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