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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
Using IR and Raman spectra to explain the catalytic activity of the Fe(II)/Fe(III) pair toward the cleavage of
Felipe G Camacho1, Wagner A Alves1
1Departamento de Química Inorgânica, Instituto de Química, Universidade Federal do Rio de Janeiro, Caixa Postal 68563, Rio de Janeiro, RJ 21941-909, Brazil.
Abstract:
IR and Raman experiments of formamide (FA) solutions containing variable amounts of Fe(II) and Fe(III) salts were carried out. The νCO vibration is downshifted whereas the νCN mode is upshifted in the presence of the divalent ion. As the trivalent ion is added to the solvent, upshifts of both νCO and νCN vibrations are observed. These spectral patterns are related to the distinct FA forms that are stabilized by each ion. Fe(II) is surrounded by 6 ionic FA species while neutral ones coordinate to the trivalent ion with formation of [Fe(FA)3Cl](2+) and [Fe(FA)2(Cl)2](+). In higher salt compositions [FeCl4](-) is also identified in the spectra. Our vibrational results are very well corroborated by biological studies on the catalytic activity of the Fe(II)/Fe(III) pair in oxidative cleavage processes of polypeptides and proteins.
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