Activation of Isolated NADH:Ubiquinone Reductase I (Complex I) fromEscherichia coliby Detergent and Phospholipids. Recovery of Ubiquinone Reductase Activity and Changes in EPR Signals of Iron−Sulfur Clusters†

Biochemistry ◽  
2005 ◽  
Vol 44 (23) ◽  
pp. 8500-8506 ◽  
Author(s):  
Liliya Sinegina ◽  
Mårten Wikström ◽  
Michael I. Verkhovsky ◽  
Marina L. Verkhovskaya
Keyword(s):  
Complex I ◽  
Reductase Activity ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur ◽  
Nadh:Ubiquinone Reductase

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

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

Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation

2001 ◽  
Vol 359 (1) ◽  
pp. 139-145 ◽  
Author(s):  
Natalia A. RIOBÓ ◽  
Emilio CLEMENTI ◽  
Mariana MELANI ◽  
Alberto BOVERIS ◽  
Enrique CADENAS ◽  
...  
Keyword(s):  
Complex I ◽  
Superoxide Radical ◽  
Reductase Activity ◽  
Complex Iii ◽  
Submitochondrial Particles ◽  
Nadh:Ubiquinone Reductase ◽  
Complex I Activity ◽  
State Concentration ◽  
The Brain

This study was aimed at assessing the effects of long-term exposure to NO of respiratory activities in mitochondria from different tissues (with different ubiquinol contents), under conditions that either promote or prevent the formation of peroxynitrite. Mitochondria and submitochondrial particles isolated from rat heart, liver and brain were exposed either to a steady-state concentration or to a bolus addition of NO. NO induced the mitochondrial production of superoxide anions, hydrogen peroxide and peroxynitrite, the latter shown by nitration of mitochondrial proteins. Long-term incubation of mitochondrial membranes with NO resulted in a persistent inhibition of NADH:cytochrome c reductase activity, interpreted as inhibition of NADH:ubiquinone reductase (Complex I) activity, whereas succinate:cytochrome c reductase activity, including Complex II and Complex III electron transfer, remained unaffected. This selective effect of NO and derived species was partially prevented by superoxide dismutase and uric acid. In addition, peroxynitrite mimicked the effect of NO, including tyrosine nitration of some Complex I proteins. These results seem to indicate that the inhibition of NADH:ubiquinone reductase (Complex I) activity depends on the NO-induced generation of superoxide radical and peroxynitrite and that Complex I is selectively sensitive to peroxynitrite. Inhibition of Complex I activity by peroxynitrite may have critical implications for energy supply in tissues such as the brain, whose mitochondrial function depends largely on the channelling of reducing equivalents through Complex I.

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.

Functional sulfurtransferase is associated with mitochondrial complex I fromYarrowia lipolytica, but is not required for assembly of its iron-sulfur clusters

FEBS Letters ◽  
2005 ◽  
Vol 579 (30) ◽  
pp. 6781-6785 ◽  
Author(s):  
Albina Abdrakhmanova ◽  
Krzysztof Dobrynin ◽  
Klaus Zwicker ◽  
Stefan Kerscher ◽  
Ulrich Brandt
Keyword(s):  
Complex I ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Iron Sulfur Clusters ◽  
Iron Sulfur

scholarly journals ESR studies on iron-sulfur clusters of complex II in Ascaris suum mitochondria which exhibits strong fumarate reductase activity

FEBS Letters ◽  
1988 ◽  
Vol 242 (1) ◽  
pp. 183-186 ◽  
Author(s):  
Akiko Hata-Tanaka ◽  
Kiyoshi Kita ◽  
Rieko Furushima ◽  
Hiroshi Oya ◽  
Shigeru Itoh
Keyword(s):  
Reductase Activity ◽  
Ascaris Suum ◽  
Fumarate Reductase ◽  
Iron Sulfur Clusters ◽  
Complex Ii ◽  
Iron Sulfur
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