scholarly journals The Role of Co-Enzyme Q10 in The Respiratory Chain and Some of Its Clinical Indications: A review

2021 ◽  
Vol 18 (1) ◽  
pp. 67-77
Author(s):  
Noor Al-Huda Al-Zarqy ◽  
Zeina Al-Thanoon
Antioxidants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 608
Author(s):  
Domenico Nuzzo

All cells continuously generate reactive oxygen species (ROS) through the respiratory chain during the energy metabolism process [...]


PLoS ONE ◽  
2020 ◽  
Vol 15 (4) ◽  
pp. e0231965
Author(s):  
Pingdong Liang ◽  
Xuan Fang ◽  
Yuyao Hu ◽  
Ming Yuan ◽  
Daniel A. Raba ◽  
...  

1997 ◽  
Vol 17 (1) ◽  
pp. 3-8 ◽  
Author(s):  
Julio F. Turrens

This mini-review describes the role of different mitochondrial components in the formation of reactive oxygen species under normal and pathological conditions and the effect of inhibitors and uncouplers on superoxide formation.


mBio ◽  
2015 ◽  
Vol 6 (2) ◽  
Author(s):  
Melanie A. Spero ◽  
Frank O. Aylward ◽  
Cameron R. Currie ◽  
Timothy J. Donohue

ABSTRACTThe proton-translocating NADH:quinone oxidoreductase (complex I) is a multisubunit integral membrane enzyme found in the respiratory chains of both bacteria and eukaryotic organelles. Although much research has focused on the enzyme's central role in the mitochondrial respiratory chain, comparatively little is known about its role in the diverse energetic lifestyles of different bacteria. Here, we used a phylogenomic approach to better understand the distribution of complex I across bacteria, the evolution of this enzyme, and its potential roles in shaping the physiology of different bacterial groups. By surveying 970 representative bacterial genomes, we predict complex I to be present in ~50% of bacteria. While this includes bacteria with a wide range of energetic schemes, the presence of complex I is associated with specific lifestyles, including aerobic respiration and specific types of phototrophy (bacteria with only a type II reaction center). A phylogeny of bacterial complex I revealed five main clades of enzymes whose evolution is largely congruent with the evolution of the bacterial groups that encode complex I. A notable exception includes the gammaproteobacteria, whose members encode one of two distantly related complex I enzymes predicted to participate in different types of respiratory chains (aerobic versus anaerobic). Comparative genomic analyses suggest a broad role for complex I in reoxidizing NADH produced from various catabolic reactions, including the tricarboxylic acid (TCA) cycle and fatty acid beta-oxidation. Together, these findings suggest diverse roles for complex I across bacteria and highlight the importance of this enzyme in shaping diverse physiologies across the bacterial domain.IMPORTANCELiving systems use conserved energy currencies, including a proton motive force (PMF), NADH, and ATP. The respiratory chain enzyme, complex I, connects these energy currencies by using NADH produced during nutrient breakdown to generate a PMF, which is subsequently used for ATP synthesis. Our goal is to better understand the role of complex I in bacteria, whose energetic diversity allows us to view its function in a range of biological contexts. We analyzed sequenced bacterial genomes to predict the presence, evolution, and function of complex I in bacteria. We identified five main classes of bacterial complex I and predict that different classes participate in different types of respiratory chains (aerobic and anaerobic). We also predict that complex I helps maintain a cellular redox state by reoxidizing NADH produced from central metabolism. Our findings suggest diverse roles for complex I in bacterial physiology, highlighting the need for future laboratory-based studies.


1982 ◽  
Vol 680 (1) ◽  
pp. 69-79 ◽  
Author(s):  
Q.S. Zhu ◽  
J.A. Berden ◽  
S. De Vries ◽  
E.C. Slater
Keyword(s):  

1961 ◽  
Vol 47 (3) ◽  
pp. 497-514 ◽  
Author(s):  
E.C. Slater ◽  
H. Rudney ◽  
J. Bouman ◽  
J. Links
Keyword(s):  

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