Application of electrostatic model to redox potentials of tetranuclear iron-sulfur clusters [Erratum to document cited in CA115(14):144764t]

1991 ◽  
Vol 95 (26) ◽  
pp. 10828-10828
Author(s):  
Masato Kodaka ◽  
Takenori Tomohiro ◽  
Hiroaki Okuno
Keyword(s):  
Electrostatic Model ◽  
Redox Potentials ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur

Application of electrostatic model to redox potentials of tetranuclear iron-sulfur clusters

1991 ◽  
Vol 95 (17) ◽  
pp. 6741-6744 ◽  
Author(s):  
Masato Kodaka ◽  
Takenori Tomohiro ◽  
Hiroaki Okuno
Keyword(s):  
Electrostatic Model ◽  
Redox Potentials ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur

Density Functional/Poisson-Boltzmann Calculations of Redox Potentials for Iron-Sulfur Clusters

1994 ◽  
Vol 116 (26) ◽  
pp. 11898-11914 ◽  
Author(s):  
Jean-Marie Mouesca ◽  
Jun L. Chen ◽  
Louis Noodleman ◽  
Donald Bashford ◽  
David A. Case
Keyword(s):  
Density Functional ◽  
Redox Potentials ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur ◽  
Poisson Boltzmann

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.

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