Compared with the ripple of visible Eu-based emission intensity induced by appended [FeN] spin crossover (SCO) units, as detected in the triple-stranded [EuFe()] helicate, the lanthanide-based luminescent detection of Fe spin-state equilibria could be improved significantly if the luminophore emission is shifted toward the near-infrared (NIR) domain. Replacing Eu with Nd in [NdFe()] (i) maintains the favorable SCO properties in acetonitrile [critical temperature = 322(2) K], (ii) saturates nonradiative vibrational relaxation processes in the 233-333 K range, and (iii) boosts the crucial intramolecular Nd → Fe energy transfer rate processes, which are sensitive to the spin state of the Fe metallic center. Consequently, the steady-state NIR Nd(F → I) emission of the luminophore is amplified and linearly correlated with the low-spin-[FeN] and high-spin-[FeN] mole fractions controlled by the SCO equilibrium. This paves the way for a straightforward and direct NIR luminescent reading/sensing of the Fe spin state in single molecules.
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http://dx.doi.org/10.1021/jacs.4c05546 | DOI Listing |
Plants (Basel)
February 2024
Key Laboratory of Forage and Endemic Crop Biotechnology, Ministry of Education, School of Life Sciences, Inner Mongolia University, Hohhot 010070, China.
The recognition of pathogen effectors through the nucleotide-binding leucine-rich repeat receptor (NLR) family is an important component of plant immunity. In addition to typical domains such as TIR, CC, NBS, and LRR, NLR proteins also contain some atypical integrated domains (IDs), the roles of which are rarely investigated. Here, we carefully screened the soybean () genome and identified the IDs that appeared in the soybean TNL-like proteins.
View Article and Find Full Text PDFJ Biol Chem
November 2023
Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin, USA. Electronic address:
Mitochondrial fission protein 1 (FIS1) is conserved in all eukaryotes, yet its function in metazoans is thought divergent. Structure-based sequence alignments of FIS1 revealed a conserved, but noncanonical, three-residue insert in its first tetratricopeptide repeat (TPR) suggesting a conserved function. In vertebrates, this insert is serine (S45), lysine (K46), and tyrosine (Y47).
View Article and Find Full Text PDFCell Biochem Biophys
December 2022
Structural Bioinformatics Unit, Department of Biochemistry, Shivaji University, Kolhapur, 416 004, Maharashtra, India.
Structural significance of conformational preferences and ribose ring puckering of newly discovered hyper modified nucleotide, 5'-monophosphate 2-methylthio cyclic N-threonylcarbamoyladenosine (p-msctA) have been investigated using quantum chemical semi-empirical RM1 and molecular dynamics simulation techniques. Automated geometry optimization of most stable structure of p-msctA has also been carried out with the help of abinitio (HF SCF, DFT) as well as semi empirical quantum chemical (RM1, AM1, PM3, and PM6) methods. Most stable structure of p-msctA is stabilized by intramolecular interactions between N(3)…HC(2'), N(1)…HC(16), O(13)…HC(15), and O(13)…HO(14).
View Article and Find Full Text PDFProc Natl Acad Sci U S A
June 2021
Department of Chemistry, Villanova University, Villanova, PA 19085
The 26S proteasome is the macromolecular machine responsible for the bulk of protein degradation in eukaryotic cells. As it degrades a ubiquitinated protein, the proteasome transitions from a substrate-accepting conformation (s1) to a set of substrate-processing conformations (s3 like), each stabilized by different intramolecular contacts. Tools to study these conformational changes remain limited, and although several interactions have been proposed to be important for stabilizing the proteasome's various conformations, it has been difficult to test these directly under equilibrium conditions.
View Article and Find Full Text PDFJ Mater Chem B
April 2021
Laboratory of Functionalized Molecular Solids, Ministry of Education, Anhui Key Laboratory of Chemo/Biosensing, Laboratory of Biosensing and Bioimaging (LOBAB), College of Chemistry and Materials Science, Anhui Normal University, Wuhu 241002, P. R. China.
In this study, a novel reaction-based A-A-A (acceptor-acceptor-acceptor) type two-photon fluorescent probe, BTC, is prepared using the benzothiadiazole (BTD) scaffold as the two-photon fluorophore and electron-accepting centre. Two β-chlorovinyl aldehyde moieties are symmetrically connected to both ends of the BTD scaffold and act as reaction groups to recognize SO2 and quenching groups to make the dis-activated probe stay at off-state due to their weak electron-withdrawing effect. In the presence of SO2 derivatives, the aldehyde groups are consumed through aldehyde addition, resulting in the activation of intramolecular charge transfer (ICT) processes and therefore recovering the fluorescence of the probe.
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