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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
Ionic association of hydroperoxide anion HO2- in the binding mean spherical approximation. Spectroscopic study of
Jerzy Chlistunoff1, Jean-Pierre Simonin
1Los Alamos National Laboratory, Los Alamos, NM 87544, USA. jerzy@lanl.gov
Abstract:
The ultraviolet-visible (UV-vis) spectroscopy of hydrogen peroxide in concentrated sodium hydroxide solutions was studied. The peroxide band in the UV range shifts from approximately 214 nm to approximately 236 nm as the NaOH concentration increases from 0.338 mol dm-3 to 13.1 mol dm-3. The band originates from an intramolecular electronic transition of the hydroperoxide anion HO2-, as indicated by the negligible temperature effect on the band position and confirmed by ab initio quantum mechanical calculations. It is postulated that the bathochromic shift of the peroxide band that accompanies the increase in NaOH concentration originates from the formation of the ion pair (Na+HO2-). The equilibrium constant for the ion association reaction (0.048 mol-1 dm3) and the characteristics of the individual absorption bands of the hydroperoxide anion and its associate with Na+ were determined from the numerical modeling of the absorbance data, using the binding mean spherical approximation (BIMSA).
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