scholarly journals LHON/MELAS overlap mutation in ND1 subunit of mitochondrial complex I affects ubiquinone binding as revealed by modeling in Escherichia coli NDH-1

2012 ◽  
Vol 1817 (2) ◽  
pp. 312-318 ◽  
Author(s):  
Jukka Pätsi ◽  
Pilvi Maliniemi ◽  
Salla Pakanen ◽  
Reetta Hinttala ◽  
Johanna Uusimaa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Complex I ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Ubiquinone Binding

scholarly journals Inhibitors of ROS production by the ubiquinone-binding site of mitochondrial complex I identified by chemical screening

2013 ◽  
Vol 65 ◽  
pp. 1047-1059 ◽  
Author(s):  
Adam L. Orr ◽  
Deepthi Ashok ◽  
Melissa R. Sarantos ◽  
Tong Shi ◽  
Robert E. Hughes ◽  
...  
Keyword(s):  
Binding Site ◽  
Complex I ◽  
Mitochondrial Complex I ◽  
Ros Production ◽  
Mitochondrial Complex ◽  
Chemical Screening ◽  
Ubiquinone Binding

scholarly journals Cryo-EM structure of respiratory complex I at work

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Kristian Parey ◽  
Ulrich Brandt ◽  
Hao Xie ◽  
Deryck J Mills ◽  
Karin Siegmund ◽  
...  
Keyword(s):  
Complex I ◽  
Atp Synthesis ◽  
Proton Pumping ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Membrane Protein Complex ◽  
Change Mechanism ◽  
Steady State Activity ◽  
Respiratory Complex I ◽  
Ubiquinone Binding

Mitochondrial complex I has a key role in cellular energy metabolism, generating a major portion of the proton motive force that drives aerobic ATP synthesis. The hydrophilic arm of the L-shaped ~1 MDa membrane protein complex transfers electrons from NADH to ubiquinone, providing the energy to drive proton pumping at distant sites in the membrane arm. The critical steps of energy conversion are associated with the redox chemistry of ubiquinone. We report the cryo-EM structure of complete mitochondrial complex I from the aerobic yeast Yarrowia lipolytica both in the deactive form and after capturing the enzyme during steady-state activity. The site of ubiquinone binding observed during turnover supports a two-state stabilization change mechanism for complex I.

Escherichia coli NADH dehydrogenase I, a minimal form of the mitochondrial complex I

1993 ◽  
Vol 21 (4) ◽  
pp. 998-1001 ◽  
Author(s):  
Hans Leif ◽  
Uwe Weidner ◽  
Annette Berger ◽  
Volker Spehr ◽  
Matthias Braun ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Complex I ◽  
Nadh Dehydrogenase ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Minimal Form
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