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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
New insights into the oxidative electrochemistry of vitamin E
1Division of Chemistry and Biological Chemistry, Nanyang Technological University, Singapore 637616, Singapore. webster@ntu.edu.sg
Abstract:
A combination of electrochemical and spectroscopic experiments have proven that the alpha-, beta-, gamma-, and delta-forms (vitamers) of the tocopherols (vitamin E) undergo a series of chemically reversible proton- and electron-transfer steps in dry organic solvents, such as acetonitrile or dichloromethane, to form cationic compounds: the cation radical, the dication, and the phenoxonium cation. The cationic compounds are extremely unusual in their high persistence compared with what is presently known about the oxidative stability of other phenols, particularly the phenoxonium cation of alpha-tocopherol, which is stable for at least several hours in nonaqueous solvents and is formed quantitatively by oxidation of the starting material at an applied potential of approximately +0.5 V vs ferrocene0/+ or with 2 mol equiv of NO+.
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