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Full-Text Articles in Inorganic Chemicals
A Novel Copper (Ii) Complex Identified As A Potent Drug Against Colorectal And Breast Cancer Cells And As A Poison Inhibitor For Human Topoisomerase Iiᶐ, Shayna Sandhaus, Rosella Taylor, Tiffany Edwards, Alexis Huddleston, Stephen J. Beebe, Alvin A. Holder
A Novel Copper (Ii) Complex Identified As A Potent Drug Against Colorectal And Breast Cancer Cells And As A Poison Inhibitor For Human Topoisomerase Iiᶐ, Shayna Sandhaus, Rosella Taylor, Tiffany Edwards, Alexis Huddleston, Stephen J. Beebe, Alvin A. Holder
Bioelectrics Publications
A novel complex, [Cu(acetylethTSC)Cl]Cl · 0.25C2H5OH 1 (where acetylethTSC = (E)-N-ethyl-2-[1-(thiazol-2-yl)ethylidene]hydrazinecarbothioamide), was shown to have anti-proliferative activity against various colon and aggressive breast cancer cell lines. In vitro studies showed that complex 1 acted as a poison inhibitor of human topoisomerase IIᶐ which may account for the observed anti-cancer effects.
Thioester Hydrolysis Reactivity Of Metal Complexes, James Justin Danford
Thioester Hydrolysis Reactivity Of Metal Complexes, James Justin Danford
All Graduate Theses and Dissertations, Spring 1920 to Summer 2023
Glyoxalase II is one of two metalloenzymes found in the glyoxalase pathway and is responsible for catalyzing the hydrolysis of a thioester substrate. Its bimetallic active site is found to contain a variety of metal combinations, including Fe(III)Zn(II). A recent report indicates that human glyoxalase II, while containing a Fe(II)Zn(II) center, is catalytically active as a mononuclear Zn(II) enzyme. Detailed mechanistic studies of glyoxalase II enzymes are limited due to uncertainty in the metal ion content of recombinantly prepared samples. The research presented in this thesis is focused on gaining mechanistic insight into thioester hydrolysis promoted by well-characterized metal complexes …