ATP-dependent substrate reduction at an [Fe₈S₉] double-cubane cluster.

ABSTRACT: 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(μ₂-S)]. The double-cubane-cluster-containing enzyme is capable of reducing small molecules, such as acetylene (C₂H₂), azide (N₃^-), and hydrazine (N₂H

SUBMITTER: Jeoung JH 

PROVIDER: S-EPMC5866592 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature