Download EBOOK Spectroscopic and Theoretical Studies on the {Feno}7 Complexes of Alpha-Ketoacid-Dependent and Related Enzymes: Using Nitric Oxide as a Probe of Oxygen Reactivity. PDF for free


Download EBOOK Spectroscopic and Theoretical Studies on the {Feno}7 Complexes of Alpha-Ketoacid-Dependent and Related Enzymes: Using Nitric Oxide as a Probe of Oxygen Reactivity. PDF for free Category: Science & Geography
The author of the book: Christina Dawn Brown
Format files: PDF, EPUB, TXT, DOCX
The size of the: 14.27 MB
Language: English
ISBN-13: 9781243551788
Edition: Proquest, Umi Dissertation Publishing
Date of issue: 1 September 2011

Description of the book "Spectroscopic and Theoretical Studies on the {Feno}7 Complexes of Alpha-Ketoacid-Dependent and Related Enzymes: Using Nitric Oxide as a Probe of Oxygen Reactivity.":

Mononuclear non-heme iron enzymes catalyze a wide variety of medically, pharmaceutically and biologically relevant reactions through the activation of dioxygen at a single iron center for reaction with an organic substrate. One class of these enzymes utilizes alpha-ketoglutarate (alpha-KG) as a redox-active cosubstrate, which supplies two electrons for the activation of dioxygen at an FeII center. A combination of spectroscopic techniques including EPR, absorbance, circular dichroism (CD), magnetic CD, and variable-temperature, variable-field MCD (VTVH-MCD), in conjunction with Density Function Theory (DFT) calculations correlated to the spectroscopic data, are used to explore the reaction PDF mechanisms of a subclass of the alpha-KG-dependent enzymes that bind a fused alpha-KG cofactor and substrate or a redox-active substrate. Nitric oxide is used as a dioxygen analogue to bind to Fe II and create {FeNO}7 complexes that are chromophoric and allow for the application of these spectroscopic techniques. Specifically focusing on the segment of the reaction mechanism between the formation of the FeII-enzyme substrate complex and the formation of experimentally observed oxygen intermediates, these studies explore how modification of the 2-His-1-carboxylate facial triad iron-binding motif and the binding of these redox-active substrates ePub affect FeII reactivity with dioxygen, the mechanism of decarboxylation of the alpha-KG-cofactor, and how these modifications tune the reactivity of the enzyme. Halogenating enzymes. Recently, a new sub-class of alpha-KG-dependent oxygenases has been identified which exhibits novel reactivity, the oxidative halogenation of unactivated carbon centers. These enzymes are also structurally unique in that they do not contain the standard facial triad, as a Cl - ligand is coordinated in place of the carboxylate. Studies of the chlorinating enzymes CytC3 combined with parallel studies of Taurine Dioxygenase (TauD) and past studies of Clavaminate PDF Synthase (CS2), define a role of the carboxylate ligand of the facial triad in stabilizing water coordination via a H-bonding interaction between the non-coordinating oxygen of the carboxylate and the coordinated water. These studies also provide initial insight into the active site features that favor chlorination by CytC3 over the hydroxylation reactions occurring in related enzymes. 4-Hydroxyphenylpyruvate dioxygenase. 4-hydroxyphenylpyruvate dioxygenase (HPPD) uses the substrate 4-hydroxyphenylpyruvate (HPP), which contains an alpha-keto acid that is covalently attached to the substrate, to catalyze an electrophilic attack that results in aromatic hydroxylation. While an FeIV=O intermediate is proposed to be ePub the reactive species in converting substrate to product, the key step utilizing O 2 to generate this species is the decarboxylation of the alpha-keto acid. The general view of the O2 reaction of the alpha-keto acid dependent enzymes required the presence of a five-coordinate FeII site and bidentate coordination of alpha-keto acid. However, studies of HPPD complexed with an inhibitor reveal additional substrate interactions at the ferrous site that contribute to the decarboxylation of the alpha-keto acid. Studies of the Fe-HPPD-HPP-NO complex probe the interaction of HPP with the {FeNO}7 moiety and reveal PDF strong sigma donation from HPP, which leads to a new bridged binding mode for the Fe-HPPD-HPP-O 2 complex and a new pathway for the formation of the FeIV-oxo intermediate. Isopenicillin N-synthase. Isopenicillin N synthase (IPNS) is a unique mononuclear non-heme Fe enzyme that catalyzes the four electron oxidative double ring closure of its tripeptide substrate...

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Download EBOOK Spectroscopic and Theoretical Studies on the {Feno}7 Complexes of Alpha-Ketoacid-Dependent and Related Enzymes: Using Nitric Oxide as a Probe of Oxygen Reactivity. PDF for free



Download EBOOK Spectroscopic and Theoretical Studies on the {Feno}7 Complexes of Alpha-Ketoacid-Dependent and Related Enzymes: Using Nitric Oxide as a Probe of Oxygen Reactivity. for free

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