6ENO

Double cubane cluster oxidoreductase

Summary for 6ENO

• Entry DOI: 10.2210/pdb6eno/pdb
• Descriptor: Dehydratase family protein, Double cubane cluster, CITRIC ACID, ... (5 entities in total)
• Functional Keywords: double cubane cluster, iron-sulfur protein, acetylene reduction, oxidoreductase
• Biological source: Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
• Total number of polymer chains: 1
• Total formula weight: 48874.55

Authors

Jeoung, J.H.,Dobbek, H. (deposition date: 2017-10-05, release date: 2018-03-14, Last modification date: 2024-05-08)

Primary citation

Jeoung, J.H.,Dobbek, H.
ATP-dependent substrate reduction at an [Fe8S9] double-cubane cluster.
Proc. Natl. Acad. Sci. U.S.A., 115:2994-2999, 2018

PubMed 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 [FeS]-cluster [{FeS(SCys)}(-S)]. The double-cubane-cluster-containing enzyme is capable of reducing small molecules, such as acetylene (CH), azide (N), and hydrazine (NH). We thus present a class of metalloenzymes akin in fold, metal clusters, and reactivity to nitrogenases.

PubMed: 29507223
DOI: 10.1073/pnas.1720489115

Experimental method

X-RAY DIFFRACTION (1.635 Å)