Simultaneous synthesis of thioesters and iron–sulfur clusters in water: two universal components of energy metabolism

2020 ◽  
Vol 56 (80) ◽  
pp. 11989-11992
Author(s):  
Sebastian A. Sanden ◽  
Ruiqin Yi ◽  
Masahiko Hara ◽  
Shawn E. McGlynn
Keyword(s):  
Energy Metabolism ◽  
Thioacetic Acid ◽  
One Pot ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur ◽  
Simultaneous Synthesis

Thioesters and peptide ligated [Fe–S] clusters can be synthesized simultaneously from thioacetic acid in an aqueous one-pot reaction.

scholarly journals Correction: Simultaneous synthesis of thioesters and iron–sulfur clusters in water: two universal components of energy metabolism

2020 ◽  
Vol 56 (94) ◽  
pp. 14920-14920
Author(s):  
Sebastian A. Sanden ◽  
Ruiqin Yi ◽  
Masahiko Hara ◽  
Shawn E. McGlynn
Keyword(s):  
Energy Metabolism ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur ◽  
Simultaneous Synthesis

Correction for ‘Simultaneous synthesis of thioesters and iron–sulfur clusters in water: two universal components of energy metabolism’ by Sebastian A. Sanden et al., Chem. Commun., 2020, 56, 11989–11992, DOI: 10.1039/D0CC07078A.

scholarly journals The one-carbon pool controls mitochondrial energy metabolism via complex I and iron-sulfur clusters

2021 ◽  
Vol 7 (8) ◽  
pp. eabf0717
Author(s):  
Florian A. Schober ◽  
David Moore ◽  
Ilian Atanassov ◽  
Marco F. Moedas ◽  
Paula Clemente ◽  
...  
Keyword(s):  
Energy Metabolism ◽  
Complex I ◽  
Cancer Metabolism ◽  
Iron Sulfur Cluster ◽  
Protein Targets ◽  
Iron Sulfur Clusters ◽  
Mitochondrial Energy Metabolism ◽  
Iron Sulfur ◽  
The One ◽  
Cluster Biosynthesis

Induction of the one-carbon cycle is an early hallmark of mitochondrial dysfunction and cancer metabolism. Vital intermediary steps are localized to mitochondria, but it remains unclear how one-carbon availability connects to mitochondrial function. Here, we show that the one-carbon metabolite and methyl group donor S-adenosylmethionine (SAM) is pivotal for energy metabolism. A gradual decline in mitochondrial SAM (mitoSAM) causes hierarchical defects in fly and mouse, comprising loss of mitoSAM-dependent metabolites and impaired assembly of the oxidative phosphorylation system. Complex I stability and iron-sulfur cluster biosynthesis are directly controlled by mitoSAM levels, while other protein targets are predominantly methylated outside of the organelle before import. The mitoSAM pool follows its cytosolic production, establishing mitochondria as responsive receivers of one-carbon units. Thus, we demonstrate that cellular methylation potential is required for energy metabolism, with direct relevance for pathophysiology, aging, and cancer.

scholarly journals Fe-S cofactors in the SARS-CoV-2 RNA-dependent RNA polymerase are potential antiviral targets

Science ◽  
2021 ◽  
pp. eabi5224
Author(s):  
Nunziata Maio ◽  
Bernard A. P. Lafont ◽  
Debangsu Sil ◽  
Yan Li ◽  
J. Martin Bollinger ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Metal Binding ◽  
Rna Dependent Rna Polymerase ◽  
Iron Sulfur Clusters ◽  
Metal Binding Sites ◽  
Iron Sulfur ◽  
Cryo Electron Microscopy ◽  
Metal Cofactors ◽  
Antiviral Targets ◽  
Viral Helicase

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causal agent of coronavirus disease 2019 (COVID-19), uses an RNA-dependent RNA polymerase (RdRp) for the replication of its genome and the transcription of its genes. We found that the catalytic subunit of the RdRp, nsp12, ligates two iron-sulfur metal cofactors in sites that were modeled as zinc centers in the available cryo-electron microscopy structures of the RdRp complex. These metal binding sites are essential for replication and for interaction with the viral helicase. Oxidation of the clusters by the stable nitroxide TEMPOL caused their disassembly, potently inhibited the RdRp, and blocked SARS-CoV-2 replication in cell culture. These iron-sulfur clusters thus serve as cofactors for the SARS-CoV-2 RdRp and are targets for therapy of COVID-19.

EPR-derived structures of flavin radical and iron-sulfur clusters from Methylosinus sporium 5 reductase

2021 ◽  
Author(s):  
Han Sol Jeong ◽  
Sugyeong Hong ◽  
Hee Seon Yoo ◽  
Jin Kim ◽  
Yujeong Kim ◽  
...  
Keyword(s):  
Carbon Cycle ◽  
Crucial Role ◽  
Methane Monooxygenase ◽  
Global Carbon Cycle ◽  
Ambient Conditions ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur ◽  
Greenhouse Effects ◽  
Global Carbon ◽  
Significant Attention

Methane monooxygenase (MMO) has attracted significant attention owing to its crucial role in the global carbon cycle; it impedes greenhouse effects by converting methane to methanol under ambient conditions. The...

scholarly journals Multiple Sense and Antisense Promoters Contribute to the Regulated Expression of the isc-suf Operon for Iron-Sulfur Cluster Assembly in Rhodobacter

2019 ◽  
Vol 7 (12) ◽  
pp. 671 ◽  
Author(s):  
Xin Nie ◽  
Bernhard Remes ◽  
Gabriele Klug
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Photosynthetic Electron Transport ◽  
Regulatory Proteins ◽  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur Clusters ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Photosynthetic Complexes ◽  
The One

A multitude of biological functions relies on iron-sulfur clusters. The formation of photosynthetic complexes goes along with an additional demand for iron-sulfur clusters for bacteriochlorophyll synthesis and photosynthetic electron transport. However, photooxidative stress leads to the destruction of iron-sulfur clusters, and the released iron promotes the formation of further reactive oxygen species. A balanced regulation of iron-sulfur cluster synthesis is required to guarantee the supply of this cofactor, on the one hand, but also to limit stress, on the other hand. The phototrophic alpha-proteobacterium Rhodobacter sphaeroides harbors a large operon for iron-sulfur cluster assembly comprising the iscRS and suf genes. IscR (iron-sulfur cluster regulator) is an iron-dependent regulator of isc-suf genes and other genes with a role in iron metabolism. We applied reporter gene fusions to identify promoters of the isc-suf operon and studied their activity alone or in combination under different conditions. Gel-retardation assays showed the binding of regulatory proteins to individual promoters. Our results demonstrated that several promoters in a sense and antisense direction influenced isc-suf expression and the binding of the IscR, Irr, and OxyR regulatory proteins to individual promoters. These findings demonstrated a complex regulatory network of several promoters and regulatory proteins that helped to adjust iron-sulfur cluster assembly to changing conditions in Rhodobacter sphaeroides.

scholarly journals Assembly of Iron-Sulfur Clusters

1998 ◽  
Vol 273 (21) ◽  
pp. 13264-13272 ◽  
Author(s):  
Limin Zheng ◽  
Valerie L. Cash ◽  
Dennis H. Flint ◽  
Dennis R. Dean
Keyword(s):  
Iron Sulfur Clusters ◽  
Iron Sulfur
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