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

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

scholarly journals Theoretical Study on Redox Potential Control of Iron-Sulfur Cluster by Hydrogen Bonds: A Possibility of Redox Potential Programming

Molecules ◽  
2021 ◽  
Vol 26 (20) ◽  
pp. 6129
Author(s):  
Iori Era ◽  
Yasutaka Kitagawa ◽  
Natsumi Yasuda ◽  
Taigo Kamimura ◽  
Naoka Amamizu ◽  
...  
Keyword(s):  
Hydrogen Bonds ◽  
Redox Potential ◽  
Active Site ◽  
Density Functional ◽  
Redox Potentials ◽  
Iron Sulfur Cluster ◽  
Potential Control ◽  
Iron Sulfur ◽  
And Shifts ◽  
Reduced State

The effect of hydrogen bonds around the active site of Anabaena [2Fe-2S] ferredoxin (Fd) on a vertical ionization potential of the reduced state (IP(red)) is examined based on the density functional theory (DFT) calculations. The results indicate that a single hydrogen bond increases the relative stability of the reduced state, and shifts IP(red) to a reductive side by 0.31–0.33 eV, regardless of the attached sulfur atoms. In addition, the IP(red) value can be changed by the number of hydrogen bonds around the active site. The results also suggest that the redox potential of [2Fe-2S] Fd is controlled by the number of hydrogen bonds because IP(red) is considered to be a major factor in the redox potential. Furthermore, there is a possibility that the redox potentials of artificial iron-sulfur clusters can be finely controlled by the number of the hydrogen bonds attached to the sulfur atoms of the cluster.

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.

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