scholarly journals Production of Reactive Oxygen Species by Complex I (NADH:Ubiquinone Oxidoreductase) from Escherichia coli and Comparison to the Enzyme from Mitochondria†

Biochemistry ◽  
2008 ◽  
Vol 47 (12) ◽  
pp. 3964-3971 ◽  
Author(s):  
Daria Esterházy ◽  
Martin S. King ◽  
Gregory Yakovlev ◽  
Judy Hirst
Keyword(s):  
Escherichia Coli ◽  
Reactive Oxygen Species ◽  
Complex I ◽  
Reactive Oxygen ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Oxygen Species

Reactive Oxygen Species Production by Escherichia coli Respiratory Complex I

Biochemistry ◽  
2015 ◽  
Vol 54 (18) ◽  
pp. 2799-2801 ◽  
Author(s):  
Klaudia Frick ◽  
Marius Schulte ◽  
Thorsten Friedrich
Keyword(s):  
Escherichia Coli ◽  
Reactive Oxygen Species ◽  
Complex I ◽  
Reactive Oxygen Species Production ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Respiratory Complex ◽  
Respiratory Complex I ◽  
Species Production

scholarly journals A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Marius Schulte ◽  
Klaudia Frick ◽  
Emmanuel Gnandt ◽  
Sascha Jurkovic ◽  
Sabrina Burschel ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Reactive Oxygen Species ◽  
Complex I ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Respiratory Complex ◽  
Respiratory Complex I

scholarly journals Reduction of Hydrophilic Ubiquinones by the Flavin in Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I) and Production of Reactive Oxygen Species†

Biochemistry ◽  
2009 ◽  
Vol 48 (9) ◽  
pp. 2053-2062 ◽  
Author(s):  
Martin S. King ◽  
Mark S. Sharpley ◽  
Judy Hirst
Keyword(s):  
Reactive Oxygen Species ◽  
Complex I ◽  
Reactive Oxygen ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Oxygen Species

The production of reactive oxygen species by complex I

2008 ◽  
Vol 36 (5) ◽  
pp. 976-980 ◽  
Author(s):  
Judy Hirst ◽  
Martin S. King ◽  
Kenneth R. Pryde
Keyword(s):  
Reactive Oxygen Species ◽  
Complex I ◽  
Neuromuscular Diseases ◽  
Reactive Oxygen ◽  
Flavin Mononucleotide ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Oxygen Species ◽  
Quinone Binding ◽  
O2 Reduction ◽  
Reverse Electron Transport

ROS (reactive oxygen species) are considered to be a major cause of cellular oxidative stress, linked to neuromuscular diseases and aging. Complex I (NADH:ubiquinone oxidoreductase) is one of the main contributors to superoxide production by mitochondria, and knowledge of its mechanism of O2 reduction is required for the formulation of causative connections between complex I defects and pathological effects. There is evidence for two distinct (but not mutually exclusive) sites of O2 reduction by complex I. Studies of the isolated enzyme largely support the participation of the reduced flavin mononucleotide in the active site for NADH oxidation, and this mechanism is supported in mitochondria by correlations between the NAD(P)+ potential and O2 reduction. In addition, studies of intact mitochondria or submitochondrial particles have suggested a mechanism involving the quinone-binding site, supported by observations during reverse electron transport and the use of ‘Q-site’ inhibitors. Here, we discuss extant data and models for O2 reduction by complex I. We compare results from the isolated enzyme with results from intact mitochondria, aiming to identify similarities and differences between them and progress towards combining them to form a single, unified picture.

Intracellular Generation of Reactive Oxygen Species and DNA Damage in Escherichia Coli Mutants Exposed to Electromagnetic Field and X-Ray

1999 ◽  
Vol 20 (1) ◽  
pp. 45-51 ◽  
Author(s):  
Y. Yonezawa ◽  
J. Miyakoshi ◽  
H. Takebe ◽  
H. Nishioka
Keyword(s):  
Escherichia Coli ◽  
Reactive Oxygen Species ◽  
Dna Damage ◽  
Electromagnetic Field ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
X Ray

The β-adrenoceptor agonist isoproterenol promotes the activity of respiratory chain complex I and lowers cellular reactive oxygen species in fibroblasts and heart myoblasts

2011 ◽  
Vol 652 (1-3) ◽  
pp. 15-22 ◽  
Author(s):  
Domenico De Rasmo ◽  
Giuliano Gattoni ◽  
Francesco Papa ◽  
Arcangela Santeramo ◽  
Consiglia Pacelli ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Respiratory Chain ◽  
Complex I ◽  
Reactive Oxygen ◽  
Chain Complex ◽  
Oxygen Species ◽  
Respiratory Chain Complex ◽  
Adrenoceptor Agonist ◽  
Cellular Reactive Oxygen Species

scholarly journals Vesicular Formation of Trans-Ferulic Acid: an Efficient Approach to Improve the Radical Scavenging and Antimicrobial Properties

2021 ◽  
Author(s):  
Anahita Rezaeiroshan ◽  
Majid Saeedi ◽  
Katayoun Morteza-Semnani ◽  
Jafar Akbari ◽  
Akbar Hedayatizadeh-Omran ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Reactive Oxygen Species ◽  
Ferulic Acid ◽  
Reactive Oxygen Species Production ◽  
Radical Scavenging ◽  
Reactive Oxygen ◽  
Entrapment Efficiency ◽  
The Body ◽  
Oxygen Species ◽  
Species Production

Abstract Purposes Reactive oxygen species production is harmful to human’s health. The presence of antioxidants in the body may help to diminish reactive oxygen species. Trans-ferulic acid is a good antioxidant, but its low water solubility excludes its utilization. The study aims to explore whether a vesicular drug delivery could be a way to overcome the poor absorption of trans-ferulic acid hence improving its antimicrobial efficiency and antioxidant effect. Methods Niosomal vesicles containing the drug were prepared by film hydration method. The obtained vesicles were investigated in terms of morphology, size, entrapment efficiency, release behavior, cellular cytotoxicity, antioxidant, cellular protection study, and antimicrobial evaluations. Results The optimized niosomal formulation had a particle size of 158.7 nm and entrapment efficiency of 21.64%. The results showed that the optimized formulation containing 25 μM of trans-ferulic acid could enhance the viability of human foreskin fibroblast HFF cell line against reactive oxygen species production. The minimum effective dose of the plain drug and the niosomal formulation against Staphylococcus aurous (ATCC 29213) was 750 µg/mL and 375 µg/mL, respectively, and for Escherichia coli (ATCC 25922), it was 750 µg/mL and 187/5 µg/mL, respectively. The formulation could also improve the minimum bactericidal concentration of the drug in Staphylococcus aurous, Escherichia coli, and Acinobacter baumannii (ATCC 19606). Conclusion These results revealed an improvement in both antibacterial and antioxidant effects of the drug in the niosomal formulation.

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