110926-99-3Relevant academic research and scientific papers
Mechanistic Studies on Tryptophan Lyase (NosL): Identification of Cyanide as a Reaction Product
Bhandari, Dhananjay M.,Fedoseyenko, Dmytro,Begley, Tadhg P.
supporting information, p. 542 - 545 (2018/01/26)
Tryptophan lyase (NosL) catalyzes the formation of 3-methylindole-2-carboxylic acid and 3-methylindole from l-tryptophan. In this paper, we provide evidence supporting a formate radical intermediate and demonstrate that cyanide is a byproduct of the NosL-catalyzed reaction with l-tryptophan. These experiments require a major revision of the NosL mechanism and uncover an unanticipated connection between NosL and HydG, the radical SAM enzyme that forms cyanide and carbon monoxide from tyrosine during the biosynthesis of the metallo-cluster of the [Fe-Fe] hydrogenase.
[FeFe]-Hydrogenase Cyanide Ligands Derived from S-Adenosylmethionine- Dependent Cleavage of Tyrosine
Driesener, Rebecca C.,Challand, Martin R.,McGlynn, Shawn E.,Shepard, Eric M.,Boyd, Eric S.,Broderick, Joan B.,Peters, John W.,Roach, Peter L.
supporting information; experimental part, p. 1687 - 1690 (2010/06/16)
"Chemical Equation Presented" What's your poison? Hydrogenases catalyze the reversible formation of dihydrogen from two electrons and two protons. The maturation of the [FeFe]-hydrogenase active-site cofactor (H cluster) requires three gene products, HydE
