ReviewChembiochem : a European journal of chemical biology2020
Double-Cubane [8Fe9S] Clusters: A Novel Nitrogenase-Related Cofactor in Biology.
Review in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Article
- Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Review
- Article
- Eight Unexpected Selenoprotein Families in Organometallic Biochemistry in Clostridium difficile, in ABC Transport, and in Methylmercury Biosynthesis.Journal of bacteriology · 2023Article
- Structural basis for coupled ATP-driven electron transfer in the double-cubane cluster protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Determination of the Absolute Molar Mass of [Fe-S]-Containing Proteins Using Size Exclusion Chromatography-Multi-Angle Light Scattering (SEC-MALS).Biomolecules · 2022Article
- Discovery of new enzymatic functions and metabolic pathways using genomic enzymology web tools.Current opinion in biotechnology · 2021Review
- Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Double-Cubane [8Fe9S] Clusters: A Novel Nitrogenase-Related Cofactor in Biology.Chembiochem : a European journal of chemical biology · 2020Review
- Special Issue on Nitrogenases and Homologous Systems.Chembiochem : a European journal of chemical biology · 2020Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three different types of electron-transferring metallo-ATPases are able to couple ATP hydrolysis to the reduction of low-potential metal sites, thereby energizing an electron. Besides the Fe-protein known from nitrogenase and homologous enzymes, two other kinds of ATPase with different scaffolds and cofactors are used to achieve a unidirectional, energetic, uphill electron transfer to either reduce inactive Co-corrinoid-containing proteins (RACE-type activators) or a second iron-sulfur cluster-containing enzyme of a unique radical enzymes family (archerases). We have found a new cofactor in the latter enzyme family, that is, a double-cubane cluster with two [4Fe4S] subclusters bridged by a sulfido ligand. An enzyme containing this cofactor catalyzes the ATP-dependent reduction of small molecules, including acetylene. Thus, enzymes containing the double-cubane cofactor are analogous in function and share some structural features with nitrogenases.
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