Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
-Nitrosothiols (SNOs) serve as endogenous carriers and donors of NO within living cells, releasing nitrosonium ions (NO), NO, or other nitroso derivatives. In this study, we present a bioinspired {Co(NO)} complex 1 that achieved -nitrosation towards Cys residues. The incorporation of a ferrocenyl group in 1 allowed for fine-tuning of the nitrosation reaction, taking advantage of the redox ability of Cys residues. Complex 1 was synthesized and characterized, demonstrating its NO translation reactivity. Furthermore, complex 1 successfully converted Cys into -nitrosocysteine (Cys-SNO), as confirmed by UV-Vis, IR, and XAS spectroscopy. This study presents a promising approach for -nitrosation of Cys residues for further exploration in the modification of Cys-containing peptides.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1039/d3cc02784h | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Characterization of S-glycosylated glycocins containing three disulfides.
J Ind Microbiol Biotechnol
September 2025
Department of Biochemistry University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Glycocins are a growing family of ribosomally synthesized and posttranslationally modified peptides (RiPPs) that are O- and/or S-glycosylated. Using a sequence similarity network of putative glycosyltransferases, the thg biosynthetic gene cluster was identified in the genome of Thermoanaerobacterium thermosaccharolyticum. Heterologous expression in Escherichia coli showed that the glycosyltransferase (ThgS) encoded in the biosynthetic gene cluster (BGC) adds N-acetyl-glucosamine (GlcNAc) to Ser and Cys residues of ThgA.
View Article and Find Full Text PDFRepurposing disulfiram: An innovative inhibitory approach against a broad spectrum of viruses.
Biochem Biophys Res Commun
September 2025
Department of Clinical Laboratory Medicine, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Jinan, Shandong, China; Department of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University & Shandon
Disulfiram (DSF), an FDA-approved therapeutic agent for alcohol dependence, has recently attracted considerable interest due to its broad-spectrum inhibitory effects against various viruses. Increasing evidence suggests that DSF can inhibit viral replication through two major mechanisms: the inhibition of viral protein catalytic activity and the ejection of Zn from viral proteins. This review comprehensively summarized the molecular mechanisms underlying DSF's antiviral activity against viruses such as severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), hepatitis C virus (HCV), influenza virus, human immunodeficiency virus (HIV), and Kaposi sarcoma-associated herpes virus (KSHV), with a particular focus on its dual targeting of Cys residues and Zn coordination sites.
View Article and Find Full Text PDFDevelopment of a Liposome-Based Serological Assay for SARS-CoV-2 Variants with Special Emphasis on Coupling Chemistries Required to Maintain Protein Antigenicity.
Anal Chem
September 2025
Institute of Analytical Chemistry, Chemo- and Biosensors, University of Regensburg, Universitaetsstr. 31, Regensburg 93053, Germany.
The conjugation of proteins to the outer membranes of liposomes is a standard procedure used in bioanalytical and drug delivery approaches. Herein, we describe the development of a liposome-based surrogate assay for the quantification of SARS-CoV-2 neutralizing antibodies. Taking into consideration differences in amino acid sequences within the receptor-binding domain (RBD) of SARS-CoV-2 Spike proteins derived from five selected variants of concern (VoC), we studied the impact of coupling chemistries on physicochemical properties and antigenicity.
View Article and Find Full Text PDFA biophysical approach to studying N-terminal cysteine oxidase substrate preferences.
Methods Enzymol
August 2025
School of Chemistry, The University of Sydney, Sydney, NSW, Australia. Electronic address:
N-terminal cysteine oxidases (NCOs) regulate adaptive responses to hypoxia in animals and plants, functioning as enzymatic oxygen sensors which control the oxygen-dependant stability of proteins bearing an N-terminal cysteine residue (Nt-cys) through the N-degron pathway. However, the precise properties governing NCO activity and substrate selectivity remain poorly understood. This chapter details optimised protocols for investigating the binding interactions between 2-aminoethanethiol (cysteamine) dioxygenase (ADO), a mammalian NCO, and its Nt-cys substrates using surface plasmon resonance (SPR) spectroscopy.
View Article and Find Full Text PDFTransferring asymmetrical [2Fe2S] clusters from the mitochondrial protein MiNT to acceptor.
Int J Biol Macromol
September 2025
Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Institute of Molecular Science, Shanxi University, Taiyuan 030006, China.
NEET protein is an evolutionarily conserved protein in almost all kingdoms of life. As an important member of the NEET (Asn-Glu-Glu-Thr) superfamily, MiNT (Miner2) involved in regulating iron and reactive oxygen species (ROS) homeostasis. It contains two CDGSH (consensus sequence: C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H) domains used for binding [2Fe2S] clusters.
View Article and Find Full Text PDF