Thiol oxidation to dioxygenated sulfinic acid is catalyzed by an enzyme family characterized by a cupin fold. These proteins act on free thiol-containing molecules to generate central metabolism precursors and signaling compounds in bacteria, fungi, and animal cells. In plants and animals, they also oxidize exposed N-cysteinyl residues, directing proteins to proteolysis. Enzyme kinetics, X-ray crystallography, and spectroscopy studies prompted the formulation and testing of hypotheses about the mechanism of action and the different substrate specificity of these enzymes. Concomitantly, the physiological role of thiol dioxygenation in prokaryotes and eukaryotes has been studied through genetic and physiological approaches. Further structural characterization is necessary to enable precise and safe manipulation of thiol dioxygenases (TDOs) for therapeutic, industrial, and agricultural applications.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.tibs.2024.03.007 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Influence of the second coordination sphere on O activation by a nonheme iron(II) thiolate complex.
J Inorg Biochem
March 2025
Department of Chemistry, The Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, United States. Electronic address:
The synthesis and characterization of a new ligand, 1-(bis(pyridin-2-ylmethyl) amino)-2-methylpropane-2-thiolate (BPAS) and its nonheme iron complex, Fe(BPAS)Br (1), is reported. Reaction of 1 with O at -20 °C generates a high-spin iron(III)-hydroxide complex, [Fe(OH)(BPAS)(Br)] (2), that was characterized by UV-vis, Fe Mössbauer, and electron paramagnetic resonance (EPR) spectroscopies, and electrospray ionization mass spectrometry (ESI-MS). Density functional theory (DFT) calculations were employed to support the spectroscopic assignments.
View Article and Find Full Text PDFLow feed intake at weaning reduces intestinal glutathione levels and promotes cysteine oxidation to taurine in pigs.
J Anim Sci
January 2024
Department of Animal Sciences, Auburn University, Auburn, AL 36849, USA.
Weaning stress in pigs is associated with low feed intake and poor nutrient utilization. Cysteine is a sulfur amino acid with key roles in pig production, but how cysteine metabolism and requirements are affected by weaning stress should be better defined. The objective of this study was to determine the collective impact of weaning and feed restriction on tissue cysteine metabolism.
View Article and Find Full Text PDFA distinct co-expressed sulfurtransferase extends the physiological role of mercaptopropionate dioxygenase in Pseudomonas aeruginosa PAO1.
Biochim Biophys Acta Proteins Proteom
January 2025
Department of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, Greenville, North Carolina 27834, United States. Electronic address:
Oxidation and assimilation of persulfides in bacteria is often catalyzed by a persulfide dioxygenase and sulfurtransferase in consecutive reactions. Enzymes responsible for the oxidation of persulfides have not been clearly defined in Pseudomonas aeruginosa PAO1. The characterized mercaptopropionate dioxygenase (MDO) in P.
View Article and Find Full Text PDFTolerability and first hints for potential efficacy of motor-cognitive training under inspiratory hypoxia in health and neuropsychiatric disorders: A translational viewpoint.
Neuroprotection
September 2024
Clinical Neuroscience, Max Planck Institute for Multidisciplinary Sciences, City Campus, Göttingen, Germany.
Article Synopsis
- Hypoxia is increasingly recognized as a key factor that helps brain cells adapt to low oxygen levels and reduced metabolism, leading to what the authors call "functional hypoxia."
- The study investigates the effects of combined mild inspiratory and functional hypoxia during motor-cognitive training in a group of 20 participants, including healthy individuals and those with depression or autism spectrum disorder.
- Initial findings suggest that this training under low oxygen conditions is well-tolerated and may improve well-being, cognitive performance, physical fitness, and affect immune cell responses, warranting further research with a controlled trial to better assess the benefits.
Cysteamine dioxygenase (ADO) governs cancer cell mitochondrial redox homeostasis through proline metabolism.
Sci Adv
October 2024
Princess Margaret Cancer Centre, University Health Network, Toronto, Canada.
2-Aminoethanethiol dioxygenase (ADO) is a thiol dioxygenase that sulfinylates cysteamine and amino-terminal cysteines in polypeptides. The pathophysiological roles of ADO remain largely unknown. Here, we demonstrate that ADO expression represents a vulnerability in cancer cells, as ADO depletion led to loss of proliferative capacity and survival in cancer cells and reduced xenograft growth.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!