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The relative importance of the antioxidant and pro-oxidant activities of antioxidant vitamins is an area of current research, but vitamin C, for example, appears to have a mostly antioxidant action in the body. [7] [9] However, less data is available for other dietary antioxidants, such as polyphenol antioxidants, [10] zinc, [11] and vitamin E ...
Oxidative stress mechanisms in tissue injury. Free radical toxicity induced by xenobiotics and the subsequent detoxification by cellular enzymes (termination).. Oxidative stress reflects an imbalance between the systemic manifestation of reactive oxygen species and a biological system's ability to readily detoxify the reactive intermediates or to repair the resulting damage. [1]
The international pictogram for oxidizing chemicals. Dangerous goods label for oxidizing agents. An oxidizing agent (also known as an oxidant, oxidizer, electron recipient, or electron acceptor) is a substance in a redox chemical reaction that gains or "accepts"/"receives" an electron from a reducing agent (called the reductant, reducer, or electron donor).
Oxidation response is stimulated by a disturbance in the balance between the production of reactive oxygen species and antioxidant responses, known as oxidative stress. Active species of oxygen naturally occur in aerobic cells and have both intracellular and extracellular sources.
Two sources inspired Harman: 1) the rate of living theory, which holds that lifespan is an inverse function of metabolic rate which in turn is proportional to oxygen consumption, and 2) Rebeca Gerschman's observation that hyperbaric oxygen toxicity and radiation toxicity could be explained by the same underlying phenomenon: oxygen free radicals.
NADPH oxidase (nicotinamide adenine dinucleotide phosphate oxidase) is a membrane-bound enzyme complex that faces the extracellular space. It can be found in the plasma membrane as well as in the membranes of phagosomes used by neutrophil white blood cells to engulf microorganisms.
[18] [19] An example is the oxidation of glutathione to glutathione disulfide, both of which form a redox buffering system in the cell between the endoplasmic reticulum and the cytoplasm. yFMO is localized in the cytoplasm in order to maintain the optimum redox buffer ratio necessary for proteins containing disulfide bonds to fold properly. [18]
Glucose oxidase catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone, which then hydrolyzes into gluconic acid. In order to work as a catalyst, GOx requires a coenzyme, flavin adenine dinucleotide (FAD). FAD is a common component in biological oxidation-reduction reactions. Redox reactions involve a gain or loss of electrons from ...