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Full-Text Articles in Inorganic Chemistry
Reactions Between Zinc Metallothionein And Carbonic Anhydrase, Tyler B. J. Pinter
Reactions Between Zinc Metallothionein And Carbonic Anhydrase, Tyler B. J. Pinter
Electronic Thesis and Dissertation Repository
More than 25% of proteins require metal ion cofactors for structure or function. The interactions between metalloproteins have largely been overlooked, though these interactions ultimately govern metal localization and control metal ion homeostasis. Mammalian metallothionein (MT) is a small, cysteine-rich metalloprotein that binds numerous metal ions per protein strand. Up to seven divalent metals, such as zinc or cadmium, are wrapped into a clustered two-domain structure. This unusually high metal content places MT as an attractive candidate for studying interactions with other metal-binding proteins. This present study investigates the metal transfer reactions between MTs and other metalloproteins, using carbonic anhydrase …
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, …
Structural Motifs Of Novel Metallothionein Proteins, Duncan E K Sutherland
Structural Motifs Of Novel Metallothionein Proteins, Duncan E K Sutherland
Electronic Thesis and Dissertation Repository
Metallothioneins (MT) are a family of small cysteine rich proteins, which have been implicated in toxic metal detoxification, protection against oxidative stress, and as a metallochaperone. The most well studied member of the family is the mammalian MT, which consists of two domains: a β-domain with 9 cysteine residues, which sequesters 3 Cd2+/Zn2+, and an α-domain with 11 cysteine residues, which sequesters 4 Cd2+/Zn2+. The exact functions of MT are unknown but must relate to its metalation status. Several areas that could lead to the assignment of function include 1) the determination …