Specific hypersensitivity to volatile anesthetics in a mouse lacking Ndufs4, a subunit of mitochondrial complex I

Mitochondrion ◽  
2012 ◽  
Vol 12 (5) ◽  
pp. 566-567
Author(s):  
Phil G. Morgan ◽  
Albert Quintana ◽  
Richard D. Palmiter ◽  
Margaret M. Sedensky
Keyword(s):  
Complex I ◽  
Volatile Anesthetics ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
A Subunit

scholarly journals Altered Anesthetic Sensitivity of Mice Lacking Ndufs4, a Subunit of Mitochondrial Complex I

PLoS ONE ◽  
2012 ◽  
Vol 7 (8) ◽  
pp. e42904 ◽  
Author(s):  
Albert Quintana ◽  
Philip G. Morgan ◽  
Shane E. Kruse ◽  
Richard D. Palmiter ◽  
Margaret M. Sedensky
Keyword(s):  
Complex I ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
A Subunit

Isolation, Mapping, and Genomic Structure of an X-Linked Gene for a Subunit of Human Mitochondrial Complex I

Genomics ◽  
1996 ◽  
Vol 37 (3) ◽  
pp. 281-288 ◽  
Author(s):  
Olga Zhuchenko ◽  
Manfred Wehnert ◽  
Jennifer Bailey ◽  
Zhong Sheng Sun ◽  
Cheng Chi Lee
Keyword(s):  
Complex I ◽  
Genomic Structure ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Linked Gene ◽  
A Subunit

scholarly journals Specific Modification of a Na+ Binding Site in NADH:Quinone Oxidoreductase from Klebsiella pneumoniae with Dicyclohexylcarbodiimide

2006 ◽  
Vol 188 (9) ◽  
pp. 3264-3272 ◽  
Author(s):  
Irini Vgenopoulou ◽  
Anja C. Gemperli ◽  
Julia Steuber
Keyword(s):  
Klebsiella Pneumoniae ◽  
Complex I ◽  
Covalent Modification ◽  
Carboxyl Group ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Nadh:Quinone Oxidoreductase ◽  
Quinone Reduction ◽  
Energy Conserving ◽  
A Subunit

ABSTRACT The respiratory NADH:quinone oxidoreductase (complex I) (NDH-1) is a multisubunit enzyme that translocates protons (or in some cases Na+) across energy-conserving membranes from bacteria or mitochondria. We studied the reaction of the Na+-translocating complex I from the enterobacterium Klebsiella pneumoniae with N,N′-dicyclohexylcarbodiimide (DCCD), with the aim of identifying a subunit critical for Na+ binding. At low Na+ concentrations (0.6 mM), DCCD inhibited both quinone reduction and Na+ transport by NDH-1 concurrent with the covalent modification of a 30-kDa polypeptide. In the presence of 50 mM Na+, NDH-1 was protected from inhibition by DCCD, and the modification of the 30-kDa polypeptide with [14C]DCCD was prevented, indicating that Na+ and DCCD competed for the binding to a critical carboxyl group in NDH-1. The 30-kDa polypeptide was assigned to NuoH, the homologue of the ND1 subunit from mitochondrial complex I. It is proposed that Na+ binds to the NuoH subunit during NADH-driven Na+ transport by NDH-1.

scholarly journals GhMCS1, the Cotton Orthologue of Human GRIM-19, Is a Subunit of Mitochondrial Complex I and Associated with Cotton Fibre Growth

PLoS ONE ◽  
2016 ◽  
Vol 11 (9) ◽  
pp. e0162928
Author(s):  
Chun-Juan Dong ◽  
Ai-Min Wu ◽  
Shao-Jun Du ◽  
Kai Tang ◽  
Yun Wang ◽  
...  
Keyword(s):  
Complex I ◽  
Cotton Fibre ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Fibre Growth ◽  
A Subunit
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