52329-65-4

Basic information

• Product Name: 3-sulfinopropanoic acid
• Synonyms: 3-Sulfinopropanoic acid; propanoic acid, 3-sulfino-
• CAS NO: 52329-65-4
• Molecular Formula: C₃H₆O₄S
• Molecular Weight: 138.1423
• Mol File: 52329-65-4.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 470.2°C at 760 mmHg
• Flash Point: 238.2°C
• Density: 1.733g/cm³
• Vapor Pressure: 3.84E-10mmHg at 25°C
• Refractive Index: 1.617
• CAS DataBase Reference: 3-sulfinopropanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 3-sulfinopropanoic acid(52329-65-4)
• EPA Substance Registry System: 3-sulfinopropanoic acid(52329-65-4)

Safety Data

• Hazardous Substances Data: 52329-65-4(Hazardous Substances Data)

Upstream product

• 77711-00-3 3-(chlorosulfinyl)propanoyl chloride 
• 6291-88-9 3,3'-sulfonyldipropanoic acid 

Downstream Products

• 19955-28-3 1,2-oxathiolan-5-one 2-oxide 
• 85939-98-6 methyl 3-(methoxysulfinyl)propanoate 

Relevant articles and documents

The cysteine dioxygenase homologue from Pseudomonas aeruginosa is a 3-mercaptopropionate dioxygenase

Thiol dioxygenation is the initial oxidation step that commits a thiol to important catabolic or biosynthetic pathways. The reaction is catalyzed by a family of specific non-heme mononuclear iron proteins each of which is reported to react efficiently with only one substrate. This family of enzymes includes cysteine dioxygenase, cysteamine dioxygenase, mercaptosuccinate dioxygenase, and 3-mercaptopropionate dioxygenase. Using sequence alignment to infer cysteine dioxygenase activity, a cysteine dioxygenase homologue from Pseudomonas aeruginosa (p3MDO) has been identified. Mass spectrometry of P. aeruginosa under standard growth conditions showed that p3MDO is expressed in low levels, suggesting that this metabolic pathway is available to the organism. Purified recombinant p3MDO is able to oxidize both cysteine and 3-mercaptopropionic acid in vitro, with a marked preference for 3-mercaptopropionic acid. We therefore describe this enzyme as a 3-mercaptopropionate dioxygenase. M?ssbauer spectroscopy suggests that substrate binding to the ferrous iron isthrough the thiol but indicates that each substrate could adopt different coordination geometries. Crystallographic comparison with mammalian cysteine dioxygenase shows that the overall active site geometry is conserved but suggests that the different substrate specificity can be related to replacement of an arginine by a glutamine in the active site.

SYNTHESIS AND REACTIVITY OF ACID CHLORIDES OF ALIPHATIC β-(CHLOROSULFINYL)CARBOXYLIC ACIDS

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