First Direct In Situ EPR Spectroelectrochemical Evidence of the Superoxide Anion Radical.
Summary of "First Direct In Situ EPR Spectroelectrochemical Evidence of the Superoxide Anion Radical."
For the first time, the superoxide anion radical was formed by electrochemical reduction of oxygen and detected in situ by EPR spectroscopy without changing the temperature. The spin susceptibilities of solid superoxide solutions were measured between 280 and 4 K showing Curie behavior. The EPR results were explained in the frame of an ion association and support the formation of a loose ion pair between the superoxide anion radical and the potassium crown ether complex. An alternative explanation for the large EPR line width of the superoxide anion radical at higher temperatures is given.
Leibniz Institute for Solid State and Materials Research IFW Dresden , PF 270116, D-01171 Dresden, Germany.
This article was published in the following journal.
Name: The journal of physical chemistry. B
Medical and Biotech [MESH] Definitions
A flavoprotein enzyme that catalyzes the univalent reduction of OXYGEN using NADPH as an electron donor to create SUPEROXIDE ANION. The enzyme is dependent on a variety of CYTOCHROMES. Defects in the production of superoxide ions by enzymes such as NADPH oxidase result in GRANULOMATOUS DISEASE, CHRONIC.
An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. EC 220.127.116.11.
A potent oxidant synthesized by the cell during its normal metabolism. Peroxynitrite is formed from the reaction of two free radicals, NITRIC OXIDE and the superoxide anion (SUPEROXIDES).
Primed In Situ Labeling
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