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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
Acid-base, coordination and oxidative properties of systems containing ATP, L-histidine and Ni(II) ions
Piotr Kaczmarek1, Wojciech Szczepanik, Małgorzata Jezowska-Bojczuk
1Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383 Wrocław, Poland.
Abstract:
Potentiometric measurements of ATP-His system proved an existence of five adducts in the solution with stoichiometries ranging from H(5)(ATP)(His) to H(ATP)(His)(4-). Their formation is a consequence of electrostatic interactions only. In the ternary Ni(II)-ATP-His system, two complex species NiH(ATP)(His)(2-) and Ni(ATP)(His)(3-), were found. In the former, stacking interaction between the aromatic moiety of ATP and the imidazole ring of l-histidine is crucial to the adduct stability. All studied systems are able to generate single strand lesions of plasmid DNA in the presence of hydrogen peroxide. However, only binary systems produce linear form of DNA, which is a consequence of the accumulation of the single-stranded breaks.
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