Faculty Opinions recommendation of The roles of coenzyme A in the pyruvate:ferredoxin oxidoreductase reaction mechanism: rate enhancement of electron transfer from a radical intermediate to an iron-sulfur cluster.

Author(s):  
Wolfgang Buckel
1999 ◽  
Vol 96 (7) ◽  
pp. 4149-4153 ◽  
Author(s):  
F. Schuler ◽  
T. Yano ◽  
S. Di Bernardo ◽  
T. Yagi ◽  
V. Yankovskaya ◽  
...  

Biochemistry ◽  
2007 ◽  
Vol 46 (22) ◽  
pp. 6588-6596 ◽  
Author(s):  
Thomas Pohl ◽  
Theresa Bauer ◽  
Katerina Dörner ◽  
Stefan Stolpe ◽  
Philipp Sell ◽  
...  

2006 ◽  
Vol 53 (4) ◽  
pp. 685-691 ◽  
Author(s):  
Kamil Brzóska ◽  
Sylwia Meczyńska ◽  
Marcin Kruszewski

Iron-sulfur clusters-containing proteins participate in many cellular processes, including crucial biological events like DNA synthesis and processing of dioxygen. In most iron-sulfur proteins, the clusters function as electron-transfer groups in mediating one-electron redox processes and as such they are integral components of respiratory and photosynthetic electron transfer chains and numerous redox enzymes involved in carbon, oxygen, hydrogen, sulfur and nitrogen metabolism. Recently, novel regulatory and enzymatic functions of these proteins have emerged. Iron-sulfur cluster proteins participate in the control of gene expression, oxygen/nitrogen sensing, control of labile iron pool and DNA damage recognition and repair. Their role in cellular response to oxidative stress and as a source of free iron ions is also discussed.


Biochemistry ◽  
1997 ◽  
Vol 36 (49) ◽  
pp. 15109-15117 ◽  
Author(s):  
John K. Hurley ◽  
Anne M. Weber-Main ◽  
Anne E. Hodges ◽  
Marian T. Stankovich ◽  
Matthew M. Benning ◽  
...  

2018 ◽  
Vol 9 (41) ◽  
pp. 7948-7957 ◽  
Author(s):  
Stella A. Child ◽  
Justin M. Bradley ◽  
Tara L. Pukala ◽  
Dimitri A. Svistunenko ◽  
Nick E. Le Brun ◽  
...  

Unusual ferredoxins with different iron–sulfur cluster binding motifs support natural product biosynthesis in a wide range of bacteria.


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