6eno

Publication Abstract from PubMed

Chemically demanding reductive conversions in biology, such as the reduction of dinitrogen to ammonia or the Birch-type reduction of aromatic compounds, depend on Fe/S-cluster-containing ATPases. These reductions are typically catalyzed by two-component systems, in which an Fe/S-cluster-containing ATPase energizes an electron to reduce a metal site on the acceptor protein that drives the reductive reaction. Here, we show a two-component system featuring a double-cubane [Fe8S9]-cluster [{Fe4S4(SCys)3}2(mu2-S)]. The double-cubane-cluster-containing enzyme is capable of reducing small molecules, such as acetylene (C2H2), azide (N3(-)), and hydrazine (N2H4). We thus present a class of metalloenzymes akin in fold, metal clusters, and reactivity to nitrogenases.

ATP-dependent substrate reduction at an [Fe8S9] double-cubane cluster.,Jeoung JH, Dobbek H Proc Natl Acad Sci U S A. 2018 Mar 5. pii: 1720489115. doi:, 10.1073/pnas.1720489115. PMID:29507223^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.