scholarly journals Resistance of guinea pig cardiac cytochrome c oxidase (complex IV) to extended ischemic time during global ischemia and reperfusion

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Andrew M Wuenstel ◽  
Amadou KS Camara ◽  
James S Heisner ◽  
Mohammed Aldakkak ◽  
David F Stowe
Keyword(s):  
Cytochrome C ◽  
Guinea Pig ◽  
Cytochrome C Oxidase ◽  
Global Ischemia ◽  
Ischemia And Reperfusion ◽  
Complex Iv ◽  
Ischemic Time

scholarly journals Pathology of Mitochondrial Encephalomyopathies

2005 ◽  
Vol 32 (2) ◽  
pp. 152-166 ◽  
Author(s):  
Harvey B. Sarnat ◽  
José Marín-García
Keyword(s):  
Cytochrome C ◽  
Succinate Dehydrogenase ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Morphological Evidence ◽  
Regular Feature ◽  
Complex Iv ◽  
Genetic Studies ◽  
Mitochondrial Encephalomyopathies ◽  
Mitochondrial Cytopathy

ABSTRACT:Muscle biopsy provides the best tissue to confirm a mitochondrial cytopathy. Histochemical features often correlate with specific syndromes and facilitate the selection of biochemical and genetic studies. Ragged-red fibres nearly always indicate a combination defect of respiratory complexes I and IV. Increased punctate lipid within myofibers is a regular feature of Kearns-Sayre and PEO, but not of MELAS and MERRF. Total deficiency of succinate dehydrogenase indicates a severe defect in Complex II; total absence of cytochrome-c-oxidase activity in all myofibres correlates with a severe deficiency of Complex IV or of coenzyme-Q10. The selective loss of cytochrome-c-oxidase activity in scattered myofibers, particularly if accompanied by strong succinate dehydrogenase staining in these same fibres, is good evidence of mitochondrial cytopathy and often of a significant mtDNA mutation, though not specific for Complex IV disorders. Glycogen may be excessive in ragged-red zones. Ultrastructure provides morphological evidence of mitochondrial cytopathy, in axons and endothelial cells as well as myocytes. Abnormal axonal mitochondria may contribute to neurogenic atrophy of muscle, a secondary chronic feature. Quantitative determinations of respiratory chain enzyme complexes, with citrate synthase as an internal control, confirm the histochemical impressions or may be the only evidence of mitochondrial disease. Biological and technical artifacts may yield falsely low enzymatic activities. Genetic studies screen common point mutations in mtDNA. The brain exhibits characteristic histopathological alterations in mitochondrial diseases. Skin biopsy is useful for mitochondrial ultrastructure in smooth erector pili muscles and axons; skin fibroblasts may be grown in culture. Mitochondrial alterations occur in many nonmitochondrial diseases and also may be induced by drugs and toxins.

Cytochrome c Oxidase (Complex IV)

2013 ◽  
pp. 423-426
Author(s):  
Shelagh Ferguson-Miller
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Complex Iv

scholarly journals The Lebanese Allele in the PET100 Gene: Report on Two New Families with Cytochrome c Oxidase Deficiency

2019 ◽  
Vol 08 (03) ◽  
pp. 172-178 ◽  
Author(s):  
Hicham Mansour ◽  
Sandra Sabbagh ◽  
Sami Bizzari ◽  
Stephany El-Hayek ◽  
Eliane Chouery ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Lactic Acidosis ◽  
Developmental Delay ◽  
Cytochrome C Oxidase ◽  
Brain Magnetic Resonance Imaging ◽  
Global Developmental Delay ◽  
Mitochondrial Complex ◽  
Oxidase Deficiency ◽  
Complex Iv ◽  
Cytochrome C Oxidase Deficiency

AbstractCytochrome c oxidase deficiency is caused by mutations in any of at least 30 mitochondrial and nuclear genes involved in mitochondrial complex IV biogenesis and structure, including the recently identified PET100 gene. Here, we report two families, of which one is consanguineous, with two affected siblings each. In one family, the siblings presented with developmental delay, seizures, lactic acidosis, abnormal brain magnetic resonance imaging, and low muscle mitochondrial complex IV activity at 30%. In the other family, the two siblings, now deceased, had a history of global developmental delay, failure to thrive, muscular hypotonia, seizures, developmental regression, respiratory insufficiency, and lactic acidosis. By whole exome sequencing, a missense mutation in exon 1 of the PET100 gene (c.3G > C; [p.Met1?]) was identified in both families. A review of the clinical description and literature is discussed, highlighting the importance of this variant in the Lebanese population.

scholarly journals COX16 promotes COX2 metallation and assembly during respiratory complex IV biogenesis

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Abhishek Aich ◽  
Cong Wang ◽  
Arpita Chowdhury ◽  
Christin Ronsör ◽  
David Pacheu-Grau ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Site Formation ◽  
Mitochondrial Oxidative Phosphorylation ◽  
Assembly Lines ◽  
Complex Iv ◽  
Oxidative Phosphorylation System ◽  
Water Formation ◽  
Copper Center ◽  
Redox Centers

Cytochrome c oxidase of the mitochondrial oxidative phosphorylation system reduces molecular oxygen with redox equivalent-derived electrons. The conserved mitochondrial-encoded COX1- and COX2-subunits are the heme- and copper-center containing core subunits that catalyze water formation. COX1 and COX2 initially follow independent biogenesis pathways creating assembly modules with subunit-specific, chaperone-like assembly factors that assist in redox centers formation. Here, we find that COX16, a protein required for cytochrome c oxidase assembly, interacts specifically with newly synthesized COX2 and its copper center-forming metallochaperones SCO1, SCO2, and COA6. The recruitment of SCO1 to the COX2-module is COX16- dependent and patient-mimicking mutations in SCO1 affect interaction with COX16. These findings implicate COX16 in CuA-site formation. Surprisingly, COX16 is also found in COX1-containing assembly intermediates and COX2 recruitment to COX1. We conclude that COX16 participates in merging the COX1 and COX2 assembly lines.

Sequence Analysis of the Structural Nuclear Encoded Subunits and Assembly Genes of Cytochrome c Oxidase in a Cohort of 10 Isolated Complex IV—Deficient Patients Revealed Five Mutations

2006 ◽  
Vol 21 (6) ◽  
pp. 508-511 ◽  
Author(s):  
Marieke J.H. Coenen ◽  
Jan A.M. Smeitink ◽  
Jeanette M. Pots ◽  
Edwin van Kaauwen ◽  
Frans J.M. Trijbels ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Complex Iv

Deficiency in complex IV (cytochrome c oxidase) of the respiratory chain, presenting as a leukodystrophy in two siblings with Leigh syndrome

1995 ◽  
Vol 17 (2) ◽  
pp. 117-121 ◽  
Author(s):  
Dimitrios I. Zafeiriou ◽  
Berthold Koletzko ◽  
Wolfgang Mueller-Felber ◽  
Irene Paetzke ◽  
Georg Kueffer ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Leigh Syndrome ◽  
Complex Iv

Thorium inhibits human respiratory chain complex IV (cytochrome c oxidase)

2021 ◽  
pp. 127546
Author(s):  
Libing Yu ◽  
Zhaozhu Lin ◽  
Xuedan Cheng ◽  
Jian Chu ◽  
Xijian Li ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Respiratory Chain ◽  
Chain Complex ◽  
Respiratory Chain Complex ◽  
Complex Iv
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