Mononuclear Fe(I) and Fe(II) Acetylene Adducts and Their Reductive Protonation to Terminal Fe(IV) and Fe(V) Carbynes.

ABSTRACT: The activity of nitrogenase enzymes, which catalyze the conversion of atmospheric dinitrogen to bioavailable ammonia, is most commonly assayed by the reduction of acetylene gas to ethylene. Despite the practical importance of acetylene as a substrate, little is known concerning its binding or activation in the iron-rich active site. "Fischer-Tropsch" type coupling of non-native C₁ substrates to higher-order C_≥2 products is also known for nitrogenase, though potential metal-carbon multiply bonded intermediates remain underexplored. Here we report the activation of acetylene gas at a mononuclear tris(phosphino)silyl-iron center, (SiP₃)Fe, to give Fe(I) and Fe(II) side-on adducts, including S = 1/2 Fe^I(η²-HCCH); the latter is chara

SUBMITTER: Citek C 

PROVIDER: S-EPMC6800224 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature