Tetranuclear and binuclear iron-sulfur clusters in succinate dehydrogenase: A method of iron quantitation by formation of paramagnetic complexes

1976 ◽  
Vol 73 (3) ◽  
pp. 833-840 ◽  
Author(s):  
John C. Salerno ◽  
Tomoko Ohnishi ◽  
Joyce Lim ◽  
Tsoo E. King
1987 ◽  
pp. 473-484 ◽  
Author(s):  
Michael K. Johnson ◽  
Joyce E. Morningstar ◽  
Edna B. Kearney ◽  
Gary Cecchini ◽  
Brian A. C. Ackrell

Science ◽  
2021 ◽  
pp. eabi5224
Author(s):  
Nunziata Maio ◽  
Bernard A. P. Lafont ◽  
Debangsu Sil ◽  
Yan Li ◽  
J. Martin Bollinger ◽  
...  

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.


Author(s):  
Han Sol Jeong ◽  
Sugyeong Hong ◽  
Hee Seon Yoo ◽  
Jin Kim ◽  
Yujeong Kim ◽  
...  

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...


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