Reduction of the Iron−Sulfur Clusters in Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I) by EuII-DTPA, a Very Low Potential Reductant†

Biochemistry ◽  
2008 ◽  
Vol 47 (34) ◽  
pp. 8885-8893 ◽  
Author(s):  
Torsten Reda ◽  
Chérise D. Barker ◽  
Judy Hirst
Keyword(s):  
Complex I ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur

scholarly journals Iron sulfur clusters in complex I of Yarrowia lipolytica characterized by cw- and pulsed EPR

2012 ◽  
Vol 1817 ◽  
pp. S64
Author(s):  
Klaus Zwicker ◽  
Philipp Spindler ◽  
Volker Zickermann ◽  
Thomas Prisner ◽  
Ulrich Brandt
Keyword(s):  
Yarrowia Lipolytica ◽  
Complex I ◽  
Iron Sulfur Clusters ◽  
Pulsed Epr ◽  
Iron Sulfur

Iron−Sulfur Cluster N7 of the NADH:Ubiquinone Oxidoreductase (Complex I) Is Essential for Stability but Not Involved in Electron Transfer†

Biochemistry ◽  
2007 ◽  
Vol 46 (22) ◽  
pp. 6588-6596 ◽  
Author(s):  
Thomas Pohl ◽  
Theresa Bauer ◽  
Katerina Dörner ◽  
Stefan Stolpe ◽  
Philipp Sell ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Complex I ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

scholarly journals The multitude of iron–sulfur clusters in respiratory complex I

2016 ◽  
Vol 1857 (8) ◽  
pp. 1068-1072 ◽  
Author(s):  
Emmanuel Gnandt ◽  
Katerina Dörner ◽  
Marc F.J. Strampraad ◽  
Simon de Vries ◽  
Thorsten Friedrich
Keyword(s):  
Complex I ◽  
Iron Sulfur Clusters ◽  
Respiratory Complex ◽  
Iron Sulfur ◽  
Respiratory Complex I

scholarly journals Iron-sulfur cluster carrier proteins involved in the assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I)

2018 ◽  
Vol 111 (1) ◽  
pp. 31-45 ◽  
Author(s):  
Sabrina Burschel ◽  
Doris Kreuzer Decovic ◽  
Franziska Nuber ◽  
Marie Stiller ◽  
Maud Hofmann ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Complex I ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Carrier Proteins ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

A Possible Role for Iron-Sulfur Cluster N2 in Proton Translocation by the NADH:Ubiquinone Oxidoreductase (Complex I)

2005 ◽  
Vol 10 (2-4) ◽  
pp. 208-222 ◽  
Author(s):  
Dirk Flemming ◽  
Stefan Stolpe ◽  
Daniel Schneider ◽  
Petra Hellwig ◽  
Thorsten Friedrich
Keyword(s):  
Complex I ◽  
Proton Translocation ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

scholarly journals Disproportionate Deficiency of Iron-Sulfur Clusters and Subunits of Complex I in Mitochondrial Encephalomyopathy

1989 ◽  
Vol 25 (2) ◽  
pp. 194-201 ◽  
Author(s):  
Takashi Ichiki ◽  
Masashi Tanaka ◽  
Masanori Kobayashi ◽  
Naruji Sugiyama ◽  
Hiroshi Suzuki ◽  
...  
Keyword(s):  
Complex I ◽  
Mitochondrial Encephalomyopathy ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur

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.

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