4 datasets for Journal of Inorganic Biochemistry
Data for: Anti-leishmanial activity and cytotoxicity of a series of tris-aryl Sb(V) mandelate cyclometallate complexes
Contributors: Philip C. Andrews, Rebekah Duffin, Victoria Blair, Lukasz Kedzierski
... Experimental Data
Data for: Cobalt(II) “Scorpionate” Complexes as Models for Cobalt-Substituted Zinc Enzymes: Electronic Structure Investigation by Magnetic Circular Dichroism
Contributors: james larrabee, Nathan Rudd, Nicholas Plugis, Joshua Telser, Dale Swenson, Jurek Krzystek
... Structures of two Co(II) complexes used in this study.
Data for: Evolution of phosphotriesterase activities of the metallo-b-lactamase family: A theoretical study
Contributors: Ling Yang, Tian Wei Quan, Rong-Zhen Liao, Long-Fei Yan, Hao Zhang
... Coordinates of all the optimized geometries
Data for: Quantitative Analysis of Nucleic Acid-Metal Interactions and their Biological Implications
Contributors: Rachel Hellmann-Whitaker, Aleksandar Dimkovikj, Mallory Banton, Elizabeth Thorn, Lance McDanel, Katelin Arndt, Ana Royo Marco, Katelyn Unvert
... This data is a comprehensive quantitative analysis of nucleic acid-heavy metal interactions. Our abstract is as follows: RNA is known to interact with Mg2+ when assuming higher-ordered tertiary configurations. Structurally, when tRNA molecules interact with Mg2+, they consistently form a “L-shape” conformation each time they are synthesized. Therefore, if Mg2+ can induce tertiary structure formation, then binding to alternative cations could produce alternative tertiary configurations. By utilizing circular dichroism and mobility gel-shift assays it was observed that tRNA structure can be altered when in the presence of different divalent cationic species. Formation of these alternative structural configurations was further validated by aminoacylating these tRNA structural anomalies with their native enzyme, which resulted in markedly different degrees of activity. Thus, it was confirmed that structural changes do occur when tRNA forms complexes with different cations. To better understand these structural changes, quantitative cation binding to tRNA was determined through titrations as well as ICP-OES analysis, which indicated that the metal ions can bind to the tRNA structure in specific and non-specific ways. Lastly, it was observed through stopped-flow kinetics that tRNA can associate/dissociate from different cations to varying degrees, thus forming cation-specific complexes at unique rates.