The design of functional metallohydrogels is attractive but challenging. A rational approach is introduced for designing functional metallohydrogels using chiral ligands, a phenylalanine derivative with a pyridyl grou...
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The design of functional metallohydrogels is attractive but challenging. A rational approach is introduced for designing functional metallohydrogels using chiral ligands, a phenylalanine derivative with a pyridyl group ( l / d ‐PF). Intriguingly, the as‐prepared metallohydrogel exhibits excellent O 2 binding and activating properties. Insights into the O 2 binding pathway reveals the presence of a novel [( l + d )‐PF‐Cu 3+ ‐O 2 − ] species, which can efficiently reduce ferric cytochrome c with the reactive O 2 − by receiving an electron from reductant ascorbic acid. This study provides helpful instructions for developing new artificial systems with specific functions through the effective combination of chiral ligands with metal ions.
Understanding uranium-protein interaction is important for revealing the mechanism of uranyl ion(UO2+2)toxicity. In this study, we investigated the interaction between UO2+2and a quadruple mutant of cytochrome b5(E44/...
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Understanding uranium-protein interaction is important for revealing the mechanism of uranyl ion(UO2+2)toxicity. In this study, we investigated the interaction between UO2+2and a quadruple mutant of cytochrome b5(E44/48/56A/D60 A cyt b5, namely 4A cyt b5) by spectroscopic approaches. The four mutated negativelycharged surface residues of cyt b5 have been considered to be the interactive sites with cytochrome c(cyt c).Also, we studied the interaction between UO2+2and the protein-protein complex of 4A cyt b5-cyt c. The results were compared to the interaction between UO2+2and cyt b5, and the interaction between cyt c and cyt b5-cyt c complex, from previous studies. It was found that the interaction of UO2+2-cyt b5, i.e., uranyl ion binding to cyt b5 surface at Glu37 and Glu43 as previously proposed by molecular modeling, is regulated by both surface mutations of cyt b5 and its interacting protein partner cyt c. These provide valuable information on metal-protein-protein interactions and clues for understanding the mechanism of uranyl toxicity.
After publication of this article, the authors noticed that a N-C dimension error was unwillingly coded in the 3D NMR spectrum "***" processing script used to perform backbone assignments for this enzyme. Th...
After publication of this article, the authors noticed that a N-C dimension error was unwillingly coded in the 3D NMR spectrum "***" processing script used to perform backbone assignments for this enzyme. The authors noticed that some OBS, CAR and LAB values in the "***" had been switched in the y and z dimensions, probably resulting from a wrong NMRPipe selection when reading the Varian NMR experimental parameters. They have carefully re-processed, re-analyzed, re-assigned, in addition to checking all scripts to evaluate the extent of this processing error on the published assignments. Authors determined that the "***" error resulted in a significant number of incorrect backbone resonance assignments, requiring us to issue corrections in Figs. 2, 3 and 4 of this published manuscript, in addition to Table S1. New versions of these figures and table are provided below. The corresponding BMRB entry has also been revised. The authors note that these modifications do not change the global message, conclusions, and molecular dynamics simulations presented in this article. The authors are grateful to David N. Bernard (INRS) for help with finding and correcting these errors.
作者:
WHEELWRIGHT, SMScott M. Wheelwright
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