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 Investigating the function of [2Fe–2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential

2013 ◽  
Vol 456 (1) ◽  
pp. 139-146 ◽  
Author(s):  
James A. Birrell ◽  
Klaudia Morina ◽  
Hannah R. Bridges ◽  
Thorsten Friedrich ◽  
Judy Hirst
Keyword(s):  
Reactive Oxygen Species ◽  
Complex I ◽  
Reactive Oxygen Species Production ◽  
Reduction Potential ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Respiratory Complex ◽  
Respiratory Complex I ◽  
Species Production

Two residues that determine the potential of cluster N1a in respiratory complex I were identified, and their effects on its flavin-site reactions were determined. Reduction of cluster N1a by NADH does not affect reactive oxygen species production by the flavin.

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 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.

Towards the molecular mechanism of respiratory complex I

2009 ◽  
Vol 425 (2) ◽  
pp. 327-339 ◽  
Author(s):  
Judy Hirst
Keyword(s):  
Reactive Oxygen Species ◽  
Complex I ◽  
Reactive Oxygen Species Production ◽  
Reactive Oxygen ◽  
Energy Transduction ◽  
Transport Processes ◽  
Flavin Mononucleotide ◽  
Intramolecular Electron Transfer ◽  
Oxygen Species ◽  
Species Production

Complex I (NADH:quinone oxidoreductase) is crucial to respiration in many aerobic organisms. In mitochondria, it oxidizes NADH (to regenerate NAD+ for the tricarboxylic acid cycle and fatty-acid oxidation), reduces ubiquinone (the electrons are ultimately used to reduce oxygen to water) and transports protons across the mitochondrial inner membrane (to produce and sustain the protonmotive force that supports ATP synthesis and transport processes). Complex I is also a major contributor to reactive oxygen species production in the cell. Understanding the mechanisms of energy transduction and reactive oxygen species production by complex I is not only a significant intellectual challenge, but also a prerequisite for understanding the roles of complex I in disease, and for the development of effective therapies. One approach to defining a complicated reaction mechanism is to break it down into manageable parts that can be tackled individually, before being recombined and integrated to produce the complete picture. Thus energy transduction by complex I comprises NADH oxidation by a flavin mononucleotide, intramolecular electron transfer from the flavin to bound quinone along a chain of iron–sulfur clusters, quinone reduction and proton translocation. More simply, molecular oxygen is reduced by the flavin, to form the reactive oxygen species superoxide and hydrogen peroxide. The present review summarizes and evaluates experimental data that pertain to the reaction mechanisms of complex I, and describes and discusses contemporary mechanistic hypotheses, proposals and models.

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