scholarly journals Activation of Hsp90/NOS and increased NO generation does not impair mitochondrial respiratory chain by competitive binding at cytochrome C Oxidase in low oxygen concentrations

2009 ◽  
Vol 14 (6) ◽  
pp. 611-627 ◽  
Author(s):  
Tennille Presley ◽  
Kaushik Vedam ◽  
Xiaoping Liu ◽  
Jay L. Zweier ◽  
Govindasamy Ilangovan
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Competitive Binding ◽  
Low Oxygen ◽  
Mitochondrial Respiratory ◽  
Oxygen Concentrations

Carbon Monoxide Specifically Inhibits Cytochrome C Oxidase of Human Mitochondrial Respiratory Chain

2003 ◽  
Vol 93 (3) ◽  
pp. 142-146 ◽  
Author(s):  
Jose-Ramon Alonso ◽  
Francesc Cardellach ◽  
Sònia López ◽  
Jordi Casademont ◽  
Òscar Miró
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Mitochondrial Respiratory

Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide

FEBS Letters ◽  
1994 ◽  
Vol 345 (1) ◽  
pp. 50-54 ◽  
Author(s):  
M.W.J. Cleeter ◽  
J.M. Cooper ◽  
V.M. Darley-Usmar ◽  
S. Moncada ◽  
A.H.V. Schapira
Keyword(s):  
Nitric Oxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Mitochondrial Respiratory Chain ◽  
Reversible Inhibition ◽  
Mitochondrial Respiratory

New perspectives on the assembly process of mitochondrial respiratory chain complex cytochrome c oxidase

Mitochondrion ◽  
2002 ◽  
Vol 2 (1-2) ◽  
pp. 117-128 ◽  
Author(s):  
Cristina Ugalde ◽  
Marieke J.H Coenen ◽  
Murtada H Farhoud ◽  
Stefanie Gilinsky ◽  
Werner J.H Koopman ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Chain Complex ◽  
Mitochondrial Respiratory Chain ◽  
Assembly Process ◽  
Respiratory Chain Complex ◽  
Mitochondrial Respiratory Chain Complex ◽  
Mitochondrial Respiratory

scholarly journals The [PSI+] prion and HSP104 modulate cytochrome c oxidase deficiency caused by deletion of COX12

2021 ◽  
Author(s):  
Pawan Kumar Saini ◽  
Hannah Dawitz ◽  
Andreas Aufschnaiter ◽  
Jinsu Thomas ◽  
Amelie Amblard ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Experimental Evolution ◽  
Mitochondrial Respiratory Chain ◽  
Oxidase Deficiency ◽  
Functional Connection ◽  
Amyloid Aggregates ◽  
Exact Function ◽  
Mitochondrial Respiratory

Cytochrome c oxidase is a pivotal enzyme of the mitochondrial respiratory chain, which sustains bioenergetics of eukaryotic cells. Cox12, a peripheral subunit of cytochrome c oxidase, is required for full activity of the enzyme, but its exact function is unknown. Here, experimental evolution of a Saccharomyces cerevisiae Δcox12 strain for ≈300 generations allowed to restore the activity of cytochrome c oxidase. In one population, the enhanced bioenergetics was caused by a A375V mutation in the AAA+ disaggregase Hsp104. Deletion or overexpression of Hsp104 also increased respiration of the Δcox12 ancestor strain. This beneficial effect of Hsp104 was related to the loss of the [PSI+] prion, which forms cytosolic amyloid aggregates of the Sup35 protein. Overall, our data demonstrate that cytosolic aggregation of a prion impairs the mitochondrial metabolism of cells defective for Cox12. These findings identify a new functional connection between cytosolic proteostasis and biogenesis of the mitochondrial respiratory chain.

Effects of extensively oxidized low-density lipoprotein on mitochondrial function and reactive oxygen species in porcine aortic endothelial cells

2010 ◽  
Vol 298 (1) ◽  
pp. E89-E98 ◽  
Author(s):  
Subir K. Roy Chowdhury ◽  
Ganesh V. Sangle ◽  
Xueping Xie ◽  
Gerald L. Stelmack ◽  
Andrew J. Halayko ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Cardiovascular Disease ◽  
Enzyme Activity ◽  
Cytochrome C ◽  
Respiratory Chain ◽  
Complex I ◽  
Oxidized Ldl ◽  
Mitochondrial Respiratory Chain ◽  
Oxygen Species ◽  
Mitochondrial Respiratory

Atherosclerotic cardiovascular disease is the leading cause of mortality in the Western world. Dysfunction of the mitochondrial respiratory chain and overproduction of reactive oxygen species (ROS) are associated with atherosclerosis and cardiovascular disease. Oxidation increases the atherogenecity of LDL. Oxidized LDL may be apoptotic or nonapoptotic for vascular endothelial cells (EC), depending on the intensity of oxidation. A previous study demonstrated that nonapoptotic oxidized LDL increased activity of mitochondrial complex I in human umbilical vein EC. The present study examined the impact of extensively oxidized LDL (eoLDL) on oxygen consumption and the activities of key enzymes in the mitochondrial respiratory chain of cultured porcine aortic EC. Oxygraphy detected that eoLDL significantly reduced oxygen consumption in various mitochondrial complexes. Treatment with eoLDL significantly decreased NADH-ubiquinone dehydrogenase (complex I), succinate cytochrome c reductase (complex II/III), ubiquinone cytochrome c reductase (complex III), and cytochrome c oxidase (complex IV) activities and the NAD+-to-NADH ratio in EC compared with mildly oxidized LDL, LDL, or vehicle. Butylated hydroxytoluene, a potent antioxidant, normalized eoLDL-induced reductions in complex I and III enzyme activity in EC. Mitochondria-associated intracellular ROS and release of ROS from EC were significantly increased after eoLDL treatment. These findings suggest that eoLDL impairs enzyme activity in mitochondrial respiratory chain complexes and increases ROS generation from mitochondria of arterial EC. Collectively, these effects could contribute to vascular injury and atherogenesis under conditions of hypercholesterolemia and oxidative stress.

Nitric oxide and hypoxia

2007 ◽  
Vol 43 ◽  
pp. 29-42 ◽  
Author(s):  
Alexander Galkin ◽  
Annie Higgs ◽  
Salvador Moncada
Keyword(s):  
Nitric Oxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Nuclear Factor Κb ◽  
Low Oxygen ◽  
Complex Iv ◽  
Prolyl Hydroxylases ◽  
Signalling Molecules ◽  
Transport Chain ◽  
Oxygen Concentrations

NO (nitric oxide) can affect mitochondrial function by interacting with the cytochrome c oxidase (complex IV) of the electron transport chain in a manner that is reversible and in competition with oxygen. Concentrations of NO too low to inhibit respiration can trigger cell defence response mechanisms involving reactive oxygen species and various signalling molecules such as nuclear factor κB and AMP kinase. Inhibition of mitochondrial respiration by NO at low oxygen concentrations can cause so-called metabolic hypoxia and divert oxygen towards other oxygen-dependent systems. Such a diversion reactivates prolyl hydroxylases and thus accounts for the prevention by NO of the stabilization of hypoxia-inducible transcription factor. In certain circumstances NO interacts with superoxide radical to form peroxynitrite, which can affect the action of key enzymes, such as mitochondrial complex I, by S-nitrosation. This chapter discusses the physiological and pathophysiological implications of the interactions of NO with the cytochrome c oxidase.

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