Persulfides and the cellular thiol landscape [PDF]
Proceedings of the National Academy of Sciences, 2014 The biochemistry of sulfur touches on every aspect of cellular biology, from protein structure and function to redox regulation to defense against chemical stress. Over the last decade, posttranslational modification of protein thiols by reactive oxygen or nitrogen species has emerged as a major component of signal transduction, leading to both ...
Katrina M, Miranda, David A, Wink
openaire +2 more sources
Biological hydropersulfides and related polysulfides – a new concept and perspective in redox biology [PDF]
, 2018 The chemical biology of thiols (RSH, e.g., cysteine and cysteine‐containing proteins/peptides) has been a topic of extreme interest for many decades due to their reported roles in protein structure/folding, redox signaling, metal ligation, cellular ...
Akaike Takaaki +13 more
core +2 more sources
Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics [PDF]
, 2017 Cysteine hydropersulfide (CysSSH) occurs in abundant quantities in various organisms, yet little is known about its biosynthesis and physiological functions.
Akaike Takaaki +26 more
core +1 more source
Pseudomonas aeruginosa PA1006 is a persulfide-modified protein that is critical for molybdenum homeostasis. [PDF]
PLoS ONE, 2013 A companion manuscript revealed that deletion of the Pseudomonas aeruginosa (Pae) PA1006 gene caused pleiotropic defects in metabolism including a loss of all nitrate reductase activities, biofilm maturation, and virulence.
Gregory Tombline +8 more
doaj +1 more source
The Rhodanese PspE Converts Thiosulfate to Cellular Sulfane Sulfur in Escherichia coli
Antioxidants, 2023 Hydrogen sulfide (H2S) and its oxidation product zero-valent sulfur (S0) play important roles in animals, plants, and bacteria. Inside cells, S0 exists in various forms, including polysulfide and persulfide, which are collectively referred to as sulfane ...
Qiaoli Yu +6 more
doaj +1 more source
Nitrosylation of nitric-oxide-sensing regulatory proteins containing [4Fe-4S] clusters gives rise to multiple iron-nitrosyl complexes [PDF]
, 2016 The reaction of protein-bound iron–sulfur (Fe-S) clusters with nitric oxide (NO) plays key roles in NO-mediated toxicity and signaling. Elucidation of the mechanism of the reaction of NO with DNA regulatory proteins that contain Fe-S clusters has been ...
Alp, Ercan E. +13 more
core +2 more sources
TtcA a new tRNA-thioltransferase with an Fe-S cluster [PDF]
, 2014 International audienceTtcA catalyzes the post-transcriptional thiolation of cytosine 32 in some tRNAs. The enzyme from Es-cherichia coli was homologously overexpressed in E. coli.
Atta, Mohamed +6 more
core +4 more sources
Thiosulfonate‐Derived BODIPY “Stick and Glue” Strategy for Fluorescent Thiol Labeling
Angewandte Chemie, Volume 138, Issue 6, 2 February 2026.We present a powerful photochemical strategy for converting disulfide bonds into stable thioether linkages via a [1,2]‐sigmatropic rearrangement. By integrating this reaction into traditional methanethiosulfonate‐based thiol labeling, we enable light‐triggered stabilization of peptide and protein conjugates with enhanced robustness and versatility ...
Lucie Šálková +4 more
wiley +2 more sources
Frontiers in Microbiology, 2019 The mitochondrial ATP-binding cassette (ABC) transporters ABCB7 in humans, Atm1 in yeast and ATM3 in plants, are highly conserved in their overall architecture and particularly in their glutathione binding pocket located within the transmembrane spanning
Simona Riedel +6 more
doaj +1 more source
The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis
Antioxidants, 2021 Living cells have developed a relay system to efficiently transfer sulfur (S) from cysteine to various thio-cofactors (iron-sulfur (Fe-S) clusters, thiamine, molybdopterin, lipoic acid, and biotin) and thiolated tRNA. The presence of such a transit route
Mayashree Das +3 more
doaj +1 more source