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Showing 1 to 20 of 59 for “"diiron"”.
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Modeling Diiron enzymes for alkanes activation
The synthesis and characterization of a series of ruthenium 'sawhorse' complexes of the type [RU2(IJ-02CRh(CO)4(Lh]' has been successfully carried out. The complexes have been characterized by IR, 1H and 13C NMR spectroscopy, elemental analysis as well as by mass spectrometry.
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The synthesis and reactivity of thiolate bridged diiron hexacarbonyl complexes
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1987.
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Studies in biomimetic diiron(III) chemistry and zeolite-encapsulated iron complexes
Thesis (M.S.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1996.
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NMR characterization of a diiron macrocycle and structural characterization of a diketo derivative
… the macrocycle.</p><p>The NMR spectra of a diiron macrocycle, [Fe<sub>2</sub>(TIED)(CH<sub>3</sub>CN)<sub>4</sub>]<sup>4+</sup>, were examined. Temperature dependent, pH dependent, D<sup>+</sup> substitution, selectively decoupled, and COSY <sup>1</sup>H NMR experiments were performed. Two …
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Model complexes for active sites of diiron metalloproteins, dioxygen reactivity and water effects
… Metal Coordination Environment as Models for Diiron Centers in Oxygen-Dependent Non-Heme Enzymes. Utilizing hydrogen bonding interactions and sterically bulky carboxylates, synthetic routes were developed to prepare the mononuclear iron(II) complexes with the vacant coordination sites for O₂ …
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Biomimetic carboxylate-bridged diiron complexes : from solution behavior to modeling the secondary coordination sphere
… Study of Ligand Dynamics in Carboxylate-Bridged Diiron(II) Complexes Supported by a Macrocyclic Ligand A series of asymmetrically carboxylate-bridged diiron(II) complexes featuring fluorine atoms as NMR spectroscopic probes, [chemical formula ...] (10), [chemical formula ...] (11), and [chemical …
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Mechanism of assembly of the tyrosyl radical-diiron(III) cofactor of E. coli ribonucleotide reductase
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1996.
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Transformations of bridging ligands in diiron complexes: unconventional routes to new functionalized multisite bound organic frames
… possible transformations of bridging ligands in diiron complexes, in order to explore unconventional routes to the synthesis of new functionalized multisite bound organic frames. The results achieved during the Ph.D. can be summarized in the following points: 1) We have extended the assembling …
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Oxidation of substrates tethered to N-donor ligands for modeling non-heme diiron enzyme active sites
Chapter 1. Modeling Carboxylate-Rich Diiron Sites of Dioxygen-Dependent Non-Heme Enzymes Carboxylate-bridged diiron centers are employed in a variety of biological systems to activate dioxygen for substrate oxidation, and small molecule models have been synthesized to mimic this chemistry outside …
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Modeling the active sites of diiron and dicopper metalloproteins with napthyridine-, phthalazine-, and diethynylbenzene-based ligands
Chapter 1. Bio-Inspired Reactions of Diiron Centers with Dioxygen A variety of biological systems employ carboxylate-bridged diiron centers to achieve substrate oxidation using dioxygen, and numerous small molecule model compounds have been synthesized in order to mimic this chemistry in the …
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Structural studies of bacterial multicomponent monooxygenases : insights into substrate specificity, diiron center tuning and component interactions
(cont.) α-subunit cavities. The presence of 6-bromohexan-l-ol induces one of the active site helices to adopt a [pi] conformation. Together, these findings suggest modes by which molecules may move through the MMOH cavities and how both substrates and MMOB may influence the structure of the active …
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Modeling the active sites of non-heme diiron metalloproteins with sterically hindered carboxylates and syn N-Donor ligands
… the Active Sites of Carboxylate-Bridged Non-Heme Diiron Enzymes Carboxylate-bridged non-heme diiron enzymes activate dioxygen to perform a variety of biological functions. Synthetic model compounds have been prepared to gain insight into the intricacies of dioxygen activation in these enzymes. In …
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Advances in non-heme diiron modeling chemistry : developing functional protein mimics through ligand design and understanding dioxygen activation
Chapter 1 A comprehensive review of diiron modeling in the Lippard group over the past thirty years is presented. This account describes the different strategies employed to prepare biomimetic complexes of non-heme diiron protein active sites, highlighting the accomplishments of the past as well as …
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Use of sterically hindered carboxylate ligands to model structural and functional features of dioxygen-activating centers in non-heme diiron enzymes
… Modeling Dioxygen-Activating Centers in Non-Heme Diiron Enzymes: Carboxylate Shifts in Diiron(II) Complexes Supported by Sterically Hindered Carboxylate Ligands General synthetic routes are described for a series of diiron(II) complexes supported by sterically demanding carboxylate ligands …
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Magnetic properties of a diferrous-water complex and ligands for modeling the active site of MMOH
Chapter 1: The Importance of Modeling Diiron Sites in Nature.There are a variety of metalloenzymes that have nearly identical carboxylate-bridged diiron active sites. An example is sMMOH, an enzyme that catalyzes the conversion of methane to methanol. A detailed description of the active site of …
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Dioxygen activation and substrate hydroxylation by the hydroxylase component of toluene/O-xylene monooxygenase from pseudomonas sporium OX1
Non-heme carboxylate-bridged diiron centers in the hydroxylase components of the bacterial multicomponent monooxygenases activate dioxygen at structurally homologous active sites. Catalysis requires the management of four substrates: electrons, protons, dioxygen, and hydrocarbons. Protein component …
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Exploring reactivity and component interactions in Toluene/o-Xylene Monooxygenase from pseudomonas sp. OX1
… activation of dioxygen. Each BMM utilizes a diiron active site housed within a catalytic hydroxylase protein. This diiron active site is responsible for activation of dioxygen and oxidation of hydrocarbons. Additional component proteins modify the structure of the hydroxylase regulating …
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Understanding orchestrated chemical reactions in toluene/o-xylene monooxygenase from pseudomonas sporium OX1
… Versatility of Carboxylate-Bridged Nonheme- Diiron Motifs: sMMO and ToMO. Several metalloenzymes utilize a carboxylate-bridged non-heme diiron motif for dioxygen activation. Despite their conserved diiron active site structures and mechanisms of dioxygen activation, they catalyze a wide range …
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Exploring the reactivity of bacterial multicomponent monooxygenases
… at an active site carboxylate-bridged diiron center. This overview describes structural and biochemical studies of the BMM protein components, presents the proposed mechanisms of 02 activation by BMMs and related carboxylate-bridged diiron proteins, and discuses substrate reactivity of …
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Hydrogen production from model complexes of the [FeFe]- and [NiFe]-hydrogenase active sites
… in 1999. In fact, the structurally similar diiron dithiolate hexacarbonyls had been investigated since the 1920s and had well established chemistry. However, unique compared to all other diiron dithiolates, the active-site structure of [FeFe]-hydrogenase features a rotated diiron dithiolate …
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