1161949-33-2Relevant academic research and scientific papers
Iron acyl thiolato carbonyls: Structural models for the active site of the [Fe]-hydrogenase (Hmd)
Royer, Aaron M.,Salomone-Stagni, Marco,Rauchfuss, Thomas B.,Meyer-Klaucke, Wolfram
experimental part, p. 16997 - 17003 (2011/02/17)
Phosphine-modified thioester derivatives are shown to serve as efficient precursors to phosphine-stabilized ferrous acyl thiolato carbonyls, which replicate key structural features of the active site of the hydrogenase Hmd. The reaction of Ph2P
Reductive ligation mediated one-step disulfide formation of S -nitrosothiols
Zhang, Jiming,Li, Sheng,Zhang, Dehui,Wang, Hua,Whorton, A. Richard,Xian, Ming
supporting information; experimental part, p. 4208 - 4211 (2010/11/17)
A one-step reductive ligation mediated disulfide formation of S-nitrosothiols was developed. This reaction involves the reaction of the S-nitroso group with phosphine-thioesters to form sulfenamide and thiolate intermediates, which then undergo a fast intermolecular disulfide formation to form stable conjugates. This reaction can be used to design new biosensors of S-nitrosated proteins.
