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Articles 1 - 6 of 6
Full-Text Articles in Inorganic Chemistry
Impact Of The Pre-A Motif On Truncated Hemoglobin N Activity, Alexander Shayne Drena
Impact Of The Pre-A Motif On Truncated Hemoglobin N Activity, Alexander Shayne Drena
Theses and Dissertations
Tuberculosis (TB) remains the leading cause of death by an infectious agent and therefore a global health crisis, according to the most recent report by the World Health Organization. This is due, in part, to Mycobacterium tuberculosis’ impressive defensive mechanisms against immune response, as well as the rise of Multi-Drug Resistant strains that have recently developed. Towards the turn of the century, a small heme protein called truncated hemoglobin N (trHbN) was discovered to protect the bacteria against reactive nitrogen species by converting nitric oxide (NO) to nitrate at rates far exceeding those of myoglobin and closer to those of …
Biometal-Induced Structural Consequences Of Α-Synuclein – The Parkinson’S Disease Protein, Dinendra L. Abeyawardhane
Biometal-Induced Structural Consequences Of Α-Synuclein – The Parkinson’S Disease Protein, Dinendra L. Abeyawardhane
Theses and Dissertations
The pre-synaptic protein α-Synuclein (αS) is often linked to the pathology of Parkinson’s disease (PD), an age-related neurodegenerative disorder. Lewy bodies, the cytopathological hallmarks of PD, are found to be rich in aggregates of misfolded αS protein. Metal dyshomeostasis has also been linked to PD due to the accumulation of iron in the substantia nigra pars compacta, and diminished copper levels reported in this same region. Metal dyshomeostasis in the brain coupled with oxidative stress can enhance the aggregation of αS. Recently, it was confirmed that mammalian αS is universally acetylated at the N-terminus, a common post-translational modification in …
Interaction With Nitric Oxide Of The Nitrosomonas Europaea Tetraheme Protein Cytochrome C554, And Two Of Its Variants, In Increasingly Reducing Environments, Jennifer M. Mcgarry
Interaction With Nitric Oxide Of The Nitrosomonas Europaea Tetraheme Protein Cytochrome C554, And Two Of Its Variants, In Increasingly Reducing Environments, Jennifer M. Mcgarry
Theses and Dissertations
A re-investigation of the interaction with NO of the small tetraheme protein cytochrome c554 (C554) from Nitrosomonas europaea has shown that the 5-coordinate heme II of the 2-electron or 4-electron reduced protein will nitrosylate reversibly. The nitrosylation process was found to be first order in C554, first-order in NO, and second-order overall. The rate constant for NO binding to the heme was determined to be 3000 ± 140 M-1s-1, while the rate constant for dissociation was 0.034 ± 0.009 s-1; the degree of protein reduction does not appear to significantly influence the nitrosylation rate. In contrast to a previous report, …
Mechanistic Study Of Heme Protein-Mediated Nitric Oxide Dioxygenation Using Photolytically Produced Nitric Oxide, Karl Joseph Koebke
Mechanistic Study Of Heme Protein-Mediated Nitric Oxide Dioxygenation Using Photolytically Produced Nitric Oxide, Karl Joseph Koebke
Theses and Dissertations
The previously reported NO precursor [Mn(PaPy2Q)(NO)]ClO4 (1), where (PaPy2QH) is N,N-bis(2-pyridylmethyl)-amine-N-ethyl-2-quinoline-2-carboxamide, was synthesized and proven capable of producing as much as 180 µM NO when irradiated by a single 3 mJ 500nm laser pulse, in a 0.15 cm path cell, without the need for additional sacrificial reductants or oxidants. Species 1 was first used to study the reaction of nitric oxide with oxy-myoglobin (oxyMb) to form ferric myoglobin (metMb) and nitrate. This reaction had long been assumed to proceed via the same iron-bound peroxynitrite intermediate (metMb(OONO)) as the metMb-catalyzed isomerization of peroxynitrite to nitrate. Recent research showed that the metMb-catalyzed …
Cellular Zinc Trafficking: The Zinc Proteome And Its Reactions With Cadmium, Mohammad Ali Namdarghanbari
Cellular Zinc Trafficking: The Zinc Proteome And Its Reactions With Cadmium, Mohammad Ali Namdarghanbari
Theses and Dissertations
Metals play a crucial role in living systems. Iron, zinc, copper, molybdenum, and manganese are involved in many essential biological activities. Among transition metals, zinc after iron is the most abundant transition metal in the human body and the most abundant in the brain. It exists in more than 3000 proteins, which comprise about 10% of the human proteome. Zn2+ dyshomeostasis is associated with chronic diseases such as metabolic syndrome, diabetes and related complications, bone loss, growth retardation in young children, and neurological and behavioral problems. Despite a good knowledge obtained for metabolism of some metal ions such as copper, …
Towards The Use Of Time-Resolved X-Ray Crystallography In Mechanistic Studies Of Cytochrome C Nitrite Reductase From Shewanella Oneidensis, Matthew David Youngblut
Towards The Use Of Time-Resolved X-Ray Crystallography In Mechanistic Studies Of Cytochrome C Nitrite Reductase From Shewanella Oneidensis, Matthew David Youngblut
Theses and Dissertations
A high-yield expression and purification of Shewanella oneidensis cytochrome c nitrite reductase (ccNiR), and its characterization by a variety of methods, notably Laue crystallography, is reported. A key component of the expression system is an artificial ccNiR gene in which the N-terminal signal peptide from the highly expressed S. oneidensis protein "Small Tetra-heme c" replaces the wild-type signal peptide. This gene, inserted into the plasmid pHSG298 and expressed in S. oneidensis TSP-C strain, generated approximately 20 mg crude ccNiR/L culture, compared with 0.5-1 mg/L for untransformed cells. Purified ccNiR exhibited nitrite and hydroxylamine reductase activities comparable to those of E. …