ATP-dependent substrate reduction at an [Fe<sub>8</sub>S<sub>9</sub>] double-cubane cluster.
basic_science · Level V
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- Record sourced from PubMed, PMID 29507223.
- Also identified by DOI 10.1073/pnas.1720489115 and PMC identifier 5866592.
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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 [Fe<sub>8</sub>S<sub>9</sub>]-cluster [{Fe<sub>4</sub>S<sub>4</sub>(SCys)<sub>3</sub>}<sub>2</sub>(<i>μ</i><sub>2</sub>-S)]. The double-cubane-cluster-containing enzyme is capable of reducing small molecules, such as acetylene (C<sub>2</sub>H<sub>2</sub>), azide (N<sub>3</sub><sup>-</sup>), and hydrazine (N<sub>2</sub>H<sub>4</sub>). We thus present a class of metalloenzymes akin in fold, metal clusters, and reactivity to nitrogenases.
Medical subject headings
- Adenosine Triphosphate
- Iron-Sulfur Proteins